GAMT_XENTR
ID GAMT_XENTR Reviewed; 232 AA.
AC Q6PBF6; Q28HJ0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Guanidinoacetate N-methyltransferase;
DE EC=2.1.1.2;
GN Name=gamt; ORFNames=TTpA001k07.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tadpole;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2003) 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; CR760866; CAJ82893.1; -; mRNA.
DR EMBL; BC059738; AAH59738.1; -; mRNA.
DR RefSeq; NP_988896.1; NM_203565.1.
DR AlphaFoldDB; Q6PBF6; -.
DR SMR; Q6PBF6; -.
DR STRING; 8364.ENSXETP00000008001; -.
DR PaxDb; Q6PBF6; -.
DR DNASU; 394491; -.
DR GeneID; 394491; -.
DR KEGG; xtr:394491; -.
DR CTD; 2593; -.
DR Xenbase; XB-GENE-947462; gamt.
DR eggNOG; KOG1709; Eukaryota.
DR InParanoid; Q6PBF6; -.
DR OrthoDB; 1297303at2759; -.
DR Reactome; R-XTR-71288; Creatine metabolism.
DR UniPathway; UPA00104; UER00580.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000003703; Expressed in skeletal muscle tissue and 18 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; IBA:GO_Central.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0006601; P:creatine biosynthetic process; IBA:GO_Central.
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..232
FT /note="Guanidinoacetate N-methyltransferase"
FT /id="PRO_0000228968"
FT DOMAIN 1..232
FT /note="RMT2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT REGION 86..88
FT /note="S-adenosyl-L-methionine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 16
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 38
FT /ligand="guanidinoacetate"
FT /ligand_id="ChEBI:CHEBI:57742"
FT /evidence="ECO:0000250|UniProtKB:P10868,
FT 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="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 65..70
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 113..114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 131
FT /ligand="guanidinoacetate"
FT /ligand_id="ChEBI:CHEBI:57742"
FT /evidence="ECO:0000250|UniProtKB:P10868"
FT BINDING 131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 167..168
FT /ligand="guanidinoacetate"
FT /ligand_id="ChEBI:CHEBI:57742"
FT /evidence="ECO:0000250|UniProtKB:P10868"
SQ SEQUENCE 232 AA; 26575 MW; 1EB50CDD61172D4F CRC64;
MSERIFIEGE SCKSAWHNAT AGYDDTDTHL EILGKPVMER WETPYMHSLA SVAASKGGRV
LEIGFGMAIA ATKLEEYNIE EHWIIECNDG VFKRLQEWAT KQPHKIVPLK GLWEDVVPTL
PDGHFDGILY DTYPLSEETW HTHQFNFIKG HAYRLLKPGG VLTYCNLTSW GELLKAKYND
IEKMFQETQI PQLVDAGFKS ENISTTVMDL IPPEDCRYYS FKKMITPTII KV
