GAMT_BOVIN
ID GAMT_BOVIN Reviewed; 236 AA.
AC Q2TBQ3;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Guanidinoacetate N-methyltransferase;
DE EC=2.1.1.2;
GN Name=GAMT;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts guanidinoacetate to creatine, using S-
CC adenosylmethionine as the methyl donor. Important in nervous system
CC development. {ECO:0000250|UniProtKB:Q14353}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanidinoacetate + S-adenosyl-L-methionine = creatine + H(+) +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:10656, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57742, ChEBI:CHEBI:57856, ChEBI:CHEBI:57947,
CC ChEBI:CHEBI:59789; EC=2.1.1.2; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00892};
CC -!- PATHWAY: Amine and polyamine biosynthesis; creatine biosynthesis;
CC creatine from L-arginine and glycine: step 2/2.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RMT2 methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00892}.
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DR EMBL; BC109825; AAI09826.1; -; mRNA.
DR RefSeq; NP_001033633.1; NM_001038544.2.
DR AlphaFoldDB; Q2TBQ3; -.
DR SMR; Q2TBQ3; -.
DR STRING; 9913.ENSBTAP00000005375; -.
DR PaxDb; Q2TBQ3; -.
DR PeptideAtlas; Q2TBQ3; -.
DR PRIDE; Q2TBQ3; -.
DR Ensembl; ENSBTAT00000005375; ENSBTAP00000005375; ENSBTAG00000004112.
DR GeneID; 515270; -.
DR KEGG; bta:515270; -.
DR CTD; 2593; -.
DR VEuPathDB; HostDB:ENSBTAG00000004112; -.
DR VGNC; VGNC:29243; GAMT.
DR eggNOG; KOG1709; Eukaryota.
DR GeneTree; ENSGT00390000018061; -.
DR HOGENOM; CLU_102800_0_0_1; -.
DR InParanoid; Q2TBQ3; -.
DR OMA; FRRENIH; -.
DR OrthoDB; 1297303at2759; -.
DR TreeFam; TF328555; -.
DR Reactome; R-BTA-71288; Creatine metabolism.
DR UniPathway; UPA00104; UER00580.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000004112; Expressed in liver and 106 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030731; F:guanidinoacetate N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
DR GO; GO:0006601; P:creatine biosynthetic process; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016550; GuanidinoAc_N-MeTrfase.
DR InterPro; IPR026480; RMT2_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PIRSF; PIRSF009285; GAMT; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51559; SAM_RMT2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14353"
FT CHAIN 2..236
FT /note="Guanidinoacetate N-methyltransferase"
FT /id="PRO_0000228964"
FT DOMAIN 13..236
FT /note="RMT2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT REGION 90..92
FT /note="S-adenosyl-L-methionine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 20
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 42
FT /ligand="guanidinoacetate"
FT /ligand_id="ChEBI:CHEBI:57742"
FT /evidence="ECO:0000250|UniProtKB:P10868,
FT ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 46
FT /ligand="guanidinoacetate"
FT /ligand_id="ChEBI:CHEBI:57742"
FT /evidence="ECO:0000250|UniProtKB:P10868,
FT ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 50
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 69..74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 117..118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 135
FT /ligand="guanidinoacetate"
FT /ligand_id="ChEBI:CHEBI:57742"
FT /evidence="ECO:0000250|UniProtKB:P10868"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 171..172
FT /ligand="guanidinoacetate"
FT /ligand_id="ChEBI:CHEBI:57742"
FT /evidence="ECO:0000250|UniProtKB:P10868"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q14353"
SQ SEQUENCE 236 AA; 26610 MW; 18B61B459C934179 CRC64;
MSAPAATPIF APGENCSPAW RAAPAAYDAS DTHLQILGKP VMERWETPYM HALAAAAASR
GGRVLEVGFG MAIAATKVQE APIEEHWIIE CNEGVFQRLQ DWALQQPHKV VPLKGLWEEV
APTLPDSHFD GILYDTYPLS EETWHTHQFN FIRDHAFRLL KPGGVLTYCN LTSWGELMKT
KYSDITTMFE ETQVPALLEA GFRRDNIRTQ VMELVPPANC RYYAFPRMIT PLVTKH
