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Protein

Guanidinoacetate N-methyltransferase

Gene

Gamt

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Converts guanidinoacetate to creatine, using S-adenosylmethionine as the methyl donor. Important in nervous system development.By similarity

Miscellaneous

The N-terminal first 36 amino acid residues are susceptible to proteolytic cleavage, leading to loss of activity.

Catalytic activityi

S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine.PROSITE-ProRule annotation

Pathwayi: creatine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes creatine from L-arginine and glycine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glycine amidinotransferase, mitochondrial (Gatm)
  2. Guanidinoacetate N-methyltransferase (Gamt), Guanidinoacetate N-methyltransferase (Gamt)
This subpathway is part of the pathway creatine biosynthesis, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes creatine from L-arginine and glycine, the pathway creatine biosynthesis and in Amine and polyamine biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei20S-adenosyl-L-methionine1
Binding sitei42SubstratePROSITE-ProRule annotation1 Publication1
Binding sitei46SubstratePROSITE-ProRule annotation1 Publication1
Binding sitei50S-adenosyl-L-methionine1
Binding sitei135S-adenosyl-L-methionine and substrate1

GO - Molecular functioni

  • guanidinoacetate N-methyltransferase activity Source: RGD
  • protein homodimerization activity Source: RGD
  • S-adenosylmethionine-dependent methyltransferase activity Source: RGD

GO - Biological processi

  • creatine biosynthetic process Source: RGD
  • embryonic liver development Source: RGD
  • S-adenosylhomocysteine metabolic process Source: RGD
  • S-adenosylmethionine metabolic process Source: RGD

Keywordsi

Molecular functionMethyltransferase, Transferase
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-7641
BRENDAi2.1.1.2 5301
SABIO-RKiP10868
UniPathwayiUPA00104; UER00580

Names & Taxonomyi

Protein namesi
Recommended name:
Guanidinoacetate N-methyltransferase (EC:2.1.1.2)
Gene namesi
Name:Gamt
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2659 Gamt

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi46E → D: Reduces affinity for substrate and S-adenosyl-L-methionine about 2-fold. 1 Publication1
Mutagenesisi46E → Q: Reduces affinity for substrate and S-adenosyl-L-methionine about 4-fold. 1 Publication1
Mutagenesisi46E → S: Loss of activity. 1 Publication1
Mutagenesisi135D → A: Loss of activity. 1 Publication1
Mutagenesisi135D → E: Reduces affinity for S-adenosyl-L-methionine 500-fold. Reduces affinity for substrate about 40-fold. 1 Publication1
Mutagenesisi135D → N: Reduces affinity for S-adenosyl-L-methionine 2000-fold. Reduces affinity for substrate about 40-fold. 1 Publication1
Mutagenesisi222Y → F: Reduces affinity for S-adenosyl-L-methionine about 5-fold. Reduces affinity for substrate about 40-fold. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000874322 – 236Guanidinoacetate N-methyltransferaseAdd BLAST235

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei7PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP10868
PRIDEiP10868

PTM databases

iPTMnetiP10868

Expressioni

Tissue specificityi

Expressed in hepatic primordium in the embryo as soon as 12.5 days. In the adult, high levels of expression are found in liver and pancreas. Ubiquitously expressed in neuronal and glial cells in the brain.2 Publications

Interactioni

Subunit structurei

Monomer. May form homodimers upon proteolytic removal of the first 36 amino acid residues.4 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000036927

Structurei

Secondary structure

1236
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 20Combined sources4
Beta strandi33 – 36Combined sources4
Beta strandi39 – 43Combined sources5
Helixi44 – 46Combined sources3
Helixi47 – 57Combined sources11
Turni58 – 60Combined sources3
Beta strandi62 – 67Combined sources6
Helixi73 – 80Combined sources8
Beta strandi84 – 90Combined sources7
Helixi93 – 103Combined sources11
Beta strandi107 – 115Combined sources9
Helixi117 – 120Combined sources4
Helixi121 – 123Combined sources3
Beta strandi129 – 134Combined sources6
Helixi141 – 143Combined sources3
Turni144 – 146Combined sources3
Helixi147 – 154Combined sources8
Helixi156 – 159Combined sources4
Beta strandi160 – 168Combined sources9
Helixi171 – 180Combined sources10
Helixi185 – 192Combined sources8
Helixi194 – 200Combined sources7
Helixi204 – 206Combined sources3
Beta strandi207 – 213Combined sources7
Beta strandi226 – 234Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KHHX-ray2.50A/B39-236[»]
1P1BX-ray2.80A/B/C/D38-236[»]
1P1CX-ray2.50A/B38-236[»]
1XCJX-ray2.00A2-236[»]
1XCLX-ray2.00A2-236[»]
ProteinModelPortaliP10868
SMRiP10868
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10868

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 236RMT2PROSITE-ProRule annotationAdd BLAST224

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni69 – 74S-adenosyl-L-methionine binding6
Regioni90 – 92S-adenosyl-L-methionine3
Regioni117 – 118S-adenosyl-L-methionine binding2
Regioni171 – 172Substrate binding2

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. RMT2 methyltransferase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410ISNM Eukaryota
ENOG410XPX4 LUCA
HOGENOMiHOG000010290
HOVERGENiHBG005801
InParanoidiP10868

Family and domain databases

InterProiView protein in InterPro
IPR016550 GuanidinoAc_N-MeTrfase
IPR026480 RMT2_dom
IPR029063 SAM-dependent_MTases
PIRSFiPIRSF009285 GAMT, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS51559 SAM_RMT2, 1 hit

Sequencei

Sequence statusi: Complete.

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

P10868-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSAASPLF APGEDCGPAW RAAPAAYDTS DTHLQILGKP VMERWETPYM
60 70 80 90 100
HSLAAAAASR GGRVLEVGFG MAIAASRVQQ APIKEHWIIE CNDGVFQRLQ
110 120 130 140 150
NWALKQPHKV VPLKGLWEEE APTLPDGHFD GILYDTYPLS EETWHTHQFN
160 170 180 190 200
FIKTHAFRLL KPGGILTYCN LTSWGELMKS KYTDITAMFE ETQVPALLEA
210 220 230
GFQRENICTE VMALVPPADC RYYAFPQMIT PLVTKH
Length:236
Mass (Da):26,407
Last modified:January 23, 2007 - v2
Checksum:i738D6F0BC86DB1C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03588 mRNA Translation: AAA41258.1
X08056 Genomic DNA Translation: CAA30845.1
PIRiS01395
UniGeneiRn.33890

Genome annotation databases

UCSCiRGD:2659 rat

Similar proteinsi

Entry informationi

Entry nameiGAMT_RAT
AccessioniPrimary (citable) accession number: P10868
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 135 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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