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Protein

Glycine N-methyltransferase

Gene

Gnmt

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity1 Publication

Catalytic activityi

S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei22S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei31S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei34SubstratePROSITE-ProRule annotation1
Binding sitei41S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei65S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei86S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei137S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei139SubstratePROSITE-ProRule annotation1
Binding sitei176SubstratePROSITE-ProRule annotation1
Binding sitei221SubstratePROSITE-ProRule annotation1

GO - Molecular functioni

  • folic acid binding Source: UniProtKB-KW
  • glycine binding Source: UniProtKB
  • glycine N-methyltransferase activity Source: UniProtKB

GO - Biological processi

  • glycogen metabolic process Source: MGI
  • methionine metabolic process Source: MGI
  • one-carbon metabolic process Source: MGI
  • protein homotetramerization Source: UniProtKB
  • regulation of gluconeogenesis Source: MGI
  • S-adenosylmethionine metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

Folate-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.20. 3474.
ReactomeiR-MMU-389661. Glyoxylate metabolism and glycine degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycine N-methyltransferase (EC:2.1.1.20)
Gene namesi
Name:Gnmt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1202304. Gnmt.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000875252 – 293Glycine N-methyltransferaseAdd BLAST292

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylvalineBy similarity1
Modified residuei10PhosphoserineCombined sources1
Modified residuei34PhosphotyrosineCombined sources1
Modified residuei46N6-succinyllysineCombined sources1
Modified residuei191N6-succinyllysineCombined sources1
Modified residuei196N6-succinyllysineCombined sources1
Modified residuei201N6-succinyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9QXF8.
PaxDbiQ9QXF8.
PeptideAtlasiQ9QXF8.
PRIDEiQ9QXF8.

PTM databases

iPTMnetiQ9QXF8.
PhosphoSitePlusiQ9QXF8.

Expressioni

Gene expression databases

BgeeiENSMUSG00000002769.
CleanExiMM_GNMT.
GenevisibleiQ9QXF8. MM.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

IntActiQ9QXF8. 3 interactors.
MINTiMINT-1869765.
STRINGi10090.ENSMUSP00000002846.

Structurei

Secondary structure

1293
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 18Combined sources3
Turni21 – 24Combined sources4
Helixi26 – 35Combined sources10
Beta strandi39 – 41Combined sources3
Helixi43 – 55Combined sources13
Beta strandi60 – 65Combined sources6
Helixi70 – 77Combined sources8
Beta strandi81 – 87Combined sources7
Helixi89 – 101Combined sources13
Turni102 – 104Combined sources3
Helixi106 – 109Combined sources4
Beta strandi112 – 115Combined sources4
Helixi118 – 120Combined sources3
Helixi122 – 124Combined sources3
Beta strandi131 – 136Combined sources6
Helixi141 – 143Combined sources3
Beta strandi148 – 151Combined sources4
Helixi152 – 162Combined sources11
Beta strandi165 – 176Combined sources12
Helixi178 – 184Combined sources7
Beta strandi193 – 195Combined sources3
Beta strandi201 – 210Combined sources10
Beta strandi213 – 224Combined sources12
Beta strandi236 – 243Combined sources8
Helixi248 – 257Combined sources10
Turni258 – 261Combined sources4
Beta strandi263 – 273Combined sources11
Beta strandi283 – 291Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R8XX-ray2.95A/B2-293[»]
1R8YX-ray3.00A/B/C/D/E/F/G/H2-293[»]
ProteinModelPortaliQ9QXF8.
SMRiQ9QXF8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9QXF8.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni117 – 118S-adenosyl-L-methionine bindingPROSITE-ProRule annotation2

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Glycine N-methyltransferase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IF1C. Eukaryota.
ENOG410ZWXN. LUCA.
GeneTreeiENSGT00390000006845.
HOGENOMiHOG000276537.
HOVERGENiHBG051748.
InParanoidiQ9QXF8.
KOiK00552.
OMAiMITLDYT.
OrthoDBiEOG091G0J3Z.
PhylomeDBiQ9QXF8.
TreeFamiTF324814.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR014369. Gly/Sar_N_MeTrfase.
IPR025714. Methyltranfer_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR16458. PTHR16458. 1 hit.
PfamiPF13847. Methyltransf_31. 1 hit.
[Graphical view]
PIRSFiPIRSF000385. Gly_N-mtase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51600. SAM_GNMT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9QXF8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDSVYRTRS LGVAAEGLPD QYADGEAARV WQLYIGDTRS RTAEYKAWLL
60 70 80 90 100
GLLRQHGCHR VLDVACGTGV DSIMLVEEGF SVMSVDASDK MLKYALKERW
110 120 130 140 150
NRRKEPSFDN WVIEEANWLT LDKDVLSGDG FDAVICLGNS FAHLPDCKGD
160 170 180 190 200
QSEHRLALKN IASMVRPGGL LVIDHRNYDY ILSTGCAPPG KNIYYKSDLT
210 220 230 240 250
KDITTSVLTV NNKAHMVTLD YTVQVPGTGR DGSPGFSKFR LSYYPHCLAS
260 270 280 290
FTELVRAAFG GRCQHSVLGD FKPYKPGQAY VPCYFIHVLK KTD
Length:293
Mass (Da):32,675
Last modified:January 23, 2007 - v3
Checksum:i264F0ACB6BBF3CDA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti157A → E in AAH14283 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89664 mRNA. Translation: BAA88218.1.
AF325352 Genomic DNA. Translation: AAK00338.1.
AY054408 Genomic DNA. Translation: AAL06142.1.
BC014283 mRNA. Translation: AAH14283.1.
CCDSiCCDS28838.1.
RefSeqiNP_034451.1. NM_010321.1.
UniGeneiMm.29395.

Genome annotation databases

EnsembliENSMUST00000002846; ENSMUSP00000002846; ENSMUSG00000002769.
GeneIDi14711.
KEGGimmu:14711.
UCSCiuc008cue.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89664 mRNA. Translation: BAA88218.1.
AF325352 Genomic DNA. Translation: AAK00338.1.
AY054408 Genomic DNA. Translation: AAL06142.1.
BC014283 mRNA. Translation: AAH14283.1.
CCDSiCCDS28838.1.
RefSeqiNP_034451.1. NM_010321.1.
UniGeneiMm.29395.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R8XX-ray2.95A/B2-293[»]
1R8YX-ray3.00A/B/C/D/E/F/G/H2-293[»]
ProteinModelPortaliQ9QXF8.
SMRiQ9QXF8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9QXF8. 3 interactors.
MINTiMINT-1869765.
STRINGi10090.ENSMUSP00000002846.

PTM databases

iPTMnetiQ9QXF8.
PhosphoSitePlusiQ9QXF8.

Proteomic databases

MaxQBiQ9QXF8.
PaxDbiQ9QXF8.
PeptideAtlasiQ9QXF8.
PRIDEiQ9QXF8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000002846; ENSMUSP00000002846; ENSMUSG00000002769.
GeneIDi14711.
KEGGimmu:14711.
UCSCiuc008cue.1. mouse.

Organism-specific databases

CTDi27232.
MGIiMGI:1202304. Gnmt.

Phylogenomic databases

eggNOGiENOG410IF1C. Eukaryota.
ENOG410ZWXN. LUCA.
GeneTreeiENSGT00390000006845.
HOGENOMiHOG000276537.
HOVERGENiHBG051748.
InParanoidiQ9QXF8.
KOiK00552.
OMAiMITLDYT.
OrthoDBiEOG091G0J3Z.
PhylomeDBiQ9QXF8.
TreeFamiTF324814.

Enzyme and pathway databases

BRENDAi2.1.1.20. 3474.
ReactomeiR-MMU-389661. Glyoxylate metabolism and glycine degradation.

Miscellaneous databases

ChiTaRSiGnmt. mouse.
EvolutionaryTraceiQ9QXF8.
PROiQ9QXF8.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000002769.
CleanExiMM_GNMT.
GenevisibleiQ9QXF8. MM.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR014369. Gly/Sar_N_MeTrfase.
IPR025714. Methyltranfer_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR16458. PTHR16458. 1 hit.
PfamiPF13847. Methyltransf_31. 1 hit.
[Graphical view]
PIRSFiPIRSF000385. Gly_N-mtase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51600. SAM_GNMT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGNMT_MOUSE
AccessioniPrimary (citable) accession number: Q9QXF8
Secondary accession number(s): Q91WN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.