We will be switching to the new UniProt website soon. Please explore and share your feedback.
Take me to the new website.
UniProtKB - P10868 (GAMT_RAT)
Protein
Guanidinoacetate N-methyltransferase
Gene
Gamt
Organism
Rattus norvegicus (Rat)
Status
Functioni
Converts guanidinoacetate to creatine, using S-adenosylmethionine as the methyl donor. Important in nervous system development.
By similarityMiscellaneous
The N-terminal first 36 amino acid residues are susceptible to proteolytic cleavage, leading to loss of activity.
Catalytic activityi
- guanidinoacetate + S-adenosyl-L-methionine = creatine + H+ + S-adenosyl-L-homocysteinePROSITE-ProRule annotationEC:2.1.1.2PROSITE-ProRule annotation
: creatine biosynthesis Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes creatine from L-arginine and glycine. 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 20 | S-adenosyl-L-methionine | 1 | |
Binding sitei | 42 | GuanidinoacetatePROSITE-ProRule annotationCombined sources1 Publication | 1 | |
Binding sitei | 46 | GuanidinoacetatePROSITE-ProRule annotationCombined sources1 Publication | 1 | |
Binding sitei | 50 | S-adenosyl-L-methionine | 1 | |
Binding sitei | 135 | GuanidinoacetateCombined sources1 Publication | 1 | |
Binding sitei | 135 | S-adenosyl-L-methionine | 1 |
GO - Molecular functioni
- guanidinoacetate N-methyltransferase activity Source: RGD
- identical protein binding Source: RGD
- S-adenosylmethionine-dependent methyltransferase activity Source: RGD
GO - Biological processi
- animal organ morphogenesis Source: RGD
- creatine biosynthetic process Source: RGD
- embryonic liver development Source: RGD
- methylation Source: UniProtKB-KW
- regulation of multicellular organism growth Source: RGD
- S-adenosylhomocysteine metabolic process Source: RGD
- S-adenosylmethionine metabolic process Source: RGD
- spermatogenesis Source: RGD
Keywordsi
Molecular function | Methyltransferase, Transferase |
Ligand | S-adenosyl-L-methionine |
Enzyme and pathway databases
BRENDAi | 2.1.1.2, 5301 |
Reactomei | R-RNO-71288, Creatine metabolism |
SABIO-RKi | P10868 |
UniPathwayi | UPA00104;UER00580 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:Gamt |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 2659, Gamt |
Subcellular locationi
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 46 | E → D: Reduces affinity for substrate and S-adenosyl-L-methionine about 2-fold. 1 Publication | 1 | |
Mutagenesisi | 46 | E → Q: Reduces affinity for substrate and S-adenosyl-L-methionine about 4-fold. 1 Publication | 1 | |
Mutagenesisi | 46 | E → S: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 135 | D → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 135 | D → E: Reduces affinity for S-adenosyl-L-methionine 500-fold. Reduces affinity for substrate about 40-fold. 1 Publication | 1 | |
Mutagenesisi | 135 | D → N: Reduces affinity for S-adenosyl-L-methionine 2000-fold. Reduces affinity for substrate about 40-fold. 1 Publication | 1 | |
Mutagenesisi | 222 | Y → F: Reduces affinity for S-adenosyl-L-methionine about 5-fold. Reduces affinity for substrate about 40-fold. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity | |||
ChainiPRO_0000087432 | 2 – 236 | Guanidinoacetate N-methyltransferaseAdd BLAST | 235 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserineBy similarity | 1 | |
Modified residuei | 7 | PhosphoserineCombined sources | 1 |
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
PaxDbi | P10868 |
PTM databases
iPTMneti | P10868 |
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 PublicationsGO - Molecular functioni
- identical protein binding Source: RGD
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000036927 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P10868 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P10868 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 13 – 236 | RMT2PROSITE-ProRule annotationAdd BLAST | 224 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 69 – 74 | S-adenosyl-L-methionine binding | 6 | |
Regioni | 90 – 92 | S-adenosyl-L-methionine | 3 | |
Regioni | 117 – 118 | S-adenosyl-L-methionine binding | 2 | |
Regioni | 171 – 172 | Guanidinoacetate bindingCombined sources1 Publication | 2 |
Sequence similaritiesi
Belongs to the class I-like SAM-binding methyltransferase superfamily. RMT2 methyltransferase family.PROSITE-ProRule annotation
Phylogenomic databases
eggNOGi | KOG1709, Eukaryota |
InParanoidi | P10868 |
Family and domain databases
InterProi | View protein in InterPro IPR016550, GuanidinoAc_N-MeTrfase IPR026480, RMT2_dom IPR029063, SAM-dependent_MTases |
PIRSFi | PIRSF009285, GAMT, 1 hit |
SUPFAMi | SSF53335, SSF53335, 1 hit |
PROSITEi | View protein in PROSITE PS51559, SAM_RMT2, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
P10868-1 [UniParc]FASTAAdd to basket
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
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketG3V960 | G3V960_RAT | Guanidinoacetate N-methyltransferas... | Gamt rCG_29249 | 236 | Annotation score: |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J03588 mRNA Translation: AAA41258.1 X08056 Genomic DNA Translation: CAA30845.1 |
PIRi | S01395 |
Genome annotation databases
UCSCi | RGD:2659, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J03588 mRNA Translation: AAA41258.1 X08056 Genomic DNA Translation: CAA30845.1 |
PIRi | S01395 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1KHH | X-ray | 2.50 | A/B | 39-236 | [»] | |
1P1B | X-ray | 2.80 | A/B/C/D | 38-236 | [»] | |
1P1C | X-ray | 2.50 | A/B | 38-236 | [»] | |
1XCJ | X-ray | 2.00 | A | 2-236 | [»] | |
1XCL | X-ray | 2.00 | A | 2-236 | [»] | |
SMRi | P10868 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000036927 |
PTM databases
iPTMneti | P10868 |
Proteomic databases
PaxDbi | P10868 |
Genome annotation databases
UCSCi | RGD:2659, rat |
Organism-specific databases
RGDi | 2659, Gamt |
Phylogenomic databases
eggNOGi | KOG1709, Eukaryota |
InParanoidi | P10868 |
Enzyme and pathway databases
UniPathwayi | UPA00104;UER00580 |
BRENDAi | 2.1.1.2, 5301 |
Reactomei | R-RNO-71288, Creatine metabolism |
SABIO-RKi | P10868 |
Miscellaneous databases
EvolutionaryTracei | P10868 |
PROi | PR:P10868 |
Family and domain databases
InterProi | View protein in InterPro IPR016550, GuanidinoAc_N-MeTrfase IPR026480, RMT2_dom IPR029063, SAM-dependent_MTases |
PIRSFi | PIRSF009285, GAMT, 1 hit |
SUPFAMi | SSF53335, SSF53335, 1 hit |
PROSITEi | View protein in PROSITE PS51559, SAM_RMT2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | GAMT_RAT | |
Accessioni | P10868Primary (citable) accession number: P10868 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 146 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families