ID   GAMTA_XENLA             Reviewed;         233 AA.
AC   Q7ZXG7;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Guanidinoacetate N-methyltransferase A;
DE            EC=2.1.1.2;
GN   Name=gamt-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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; BC045001; AAH45001.1; -; mRNA.
DR   RefSeq; NP_001080692.1; NM_001087223.1.
DR   AlphaFoldDB; Q7ZXG7; -.
DR   SMR; Q7ZXG7; -.
DR   DNASU; 380384; -.
DR   GeneID; 380384; -.
DR   KEGG; xla:380384; -.
DR   CTD; 380384; -.
DR   Xenbase; XB-GENE-6256537; gamt.S.
DR   OMA; FRRENIH; -.
DR   OrthoDB; 1297303at2759; -.
DR   UniPathway; UPA00104; UER00580.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 380384; Expressed in kidney and 19 other tissues.
DR   GO; GO:0030731; F:guanidinoacetate N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006601; P:creatine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..233
FT                   /note="Guanidinoacetate N-methyltransferase A"
FT                   /id="PRO_0000228966"
FT   DOMAIN          1..233
FT                   /note="RMT2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT   REGION          87..89
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT   BINDING         17
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT   BINDING         39
FT                   /ligand="guanidinoacetate"
FT                   /ligand_id="ChEBI:CHEBI:57742"
FT                   /evidence="ECO:0000250|UniProtKB:P10868,
FT                   ECO:0000255|PROSITE-ProRule:PRU00892"
FT   BINDING         43
FT                   /ligand="guanidinoacetate"
FT                   /ligand_id="ChEBI:CHEBI:57742"
FT                   /evidence="ECO:0000250|UniProtKB:P10868,
FT                   ECO:0000255|PROSITE-ProRule:PRU00892"
FT   BINDING         47
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT   BINDING         66..71
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT   BINDING         114..115
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT   BINDING         132
FT                   /ligand="guanidinoacetate"
FT                   /ligand_id="ChEBI:CHEBI:57742"
FT                   /evidence="ECO:0000250|UniProtKB:P10868"
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT   BINDING         168..169
FT                   /ligand="guanidinoacetate"
FT                   /ligand_id="ChEBI:CHEBI:57742"
FT                   /evidence="ECO:0000250|UniProtKB:P10868"
SQ   SEQUENCE   233 AA;  26661 MW;  D548DA7BF1FC819C CRC64;
     MSSDKIFAEG ESCKSAWHDA TAGYDETDTH LEIMGKPVME RWETPYMHSL ATVAASKGGR
     VLEIGFGMAI AATKLEEYNI EEHWIIECND GVFKRLQEWA TKQPHKIVPL KGLWEEVVPT
     LPDGHFDGIL YDTYPLSEET WHTHQFNFIK SHAYRLLKPG GVLTYCNLTS WGELLKTKYN
     DIEKMFKETQ TPQLVDAGFK SENISTTVMD LVPPEDCRYY SFKKMITPTI TKV