GAMT_DANRE
ID GAMT_DANRE Reviewed; 234 AA.
AC Q71N41; Q3B7H3;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Guanidinoacetate N-methyltransferase;
DE EC=2.1.1.2;
GN Name=gamt; ORFNames=zgc:123136;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AB;
RA Hsiao C.D., Tsai W.Y., Tsai H.J.;
RT "Molecular cloning of zebrafish guanidinoacetate N-methyltransferase (GAMT)
RT gene.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB; TISSUE=Liver;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-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; AF425745; AAQ13341.1; -; mRNA.
DR EMBL; BC107607; AAI07608.1; -; mRNA.
DR RefSeq; NP_001099065.1; NM_001105595.1.
DR AlphaFoldDB; Q71N41; -.
DR SMR; Q71N41; -.
DR STRING; 7955.ENSDARP00000095135; -.
DR PaxDb; Q71N41; -.
DR Ensembl; ENSDART00000104360; ENSDARP00000095135; ENSDARG00000070844.
DR Ensembl; ENSDART00000193862; ENSDARP00000156721; ENSDARG00000109945.
DR GeneID; 796865; -.
DR KEGG; dre:796865; -.
DR CTD; 2593; -.
DR ZFIN; ZDB-GENE-051030-97; gamt.
DR eggNOG; KOG1709; Eukaryota.
DR GeneTree; ENSGT00390000018061; -.
DR HOGENOM; CLU_102800_0_0_1; -.
DR InParanoid; Q71N41; -.
DR OMA; FRRENIH; -.
DR OrthoDB; 1297303at2759; -.
DR PhylomeDB; Q71N41; -.
DR TreeFam; TF328555; -.
DR Reactome; R-DRE-71288; Creatine metabolism.
DR UniPathway; UPA00104; UER00580.
DR PRO; PR:Q71N41; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 11.
DR Bgee; ENSDARG00000070844; Expressed in larva and 23 other tissues.
DR ExpressionAtlas; Q71N41; baseline and differential.
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..234
FT /note="Guanidinoacetate N-methyltransferase"
FT /id="PRO_0000228965"
FT DOMAIN 1..234
FT /note="RMT2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT REGION 88..90
FT /note="S-adenosyl-L-methionine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 18
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 40
FT /ligand="guanidinoacetate"
FT /ligand_id="ChEBI:CHEBI:57742"
FT /evidence="ECO:0000250|UniProtKB:P10868,
FT ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 44
FT /ligand="guanidinoacetate"
FT /ligand_id="ChEBI:CHEBI:57742"
FT /evidence="ECO:0000250|UniProtKB:P10868,
FT ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 48
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 67..72
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 115..116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 133
FT /ligand="guanidinoacetate"
FT /ligand_id="ChEBI:CHEBI:57742"
FT /evidence="ECO:0000250|UniProtKB:P10868"
FT BINDING 133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 169..170
FT /ligand="guanidinoacetate"
FT /ligand_id="ChEBI:CHEBI:57742"
FT /evidence="ECO:0000250|UniProtKB:P10868"
FT CONFLICT 71
FT /note="I -> T (in Ref. 1; AAQ13341)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="K -> R (in Ref. 1; AAQ13341)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 234 AA; 26743 MW; C998B222A2FA1E1F CRC64;
MSAAQPIFSK GENCKQVWHD ANADYNAADT HLEIMGKPVM ERWETPYMHS LATVAASKGG
RVLEIGFGMA IAATKVESFP IEEHWIIECN DGVFQRLQEW AKSQPHKVVP LKGLWEEVAP
TLPDNHFDGI LYDTYPLSEE TWHTHQFNFI KAHAHRMLKP GGVLTYCNLT SWGELLKNKY
DNIDKMFQET QVPHLLEAGF KKEKISTTLM DISPPSECKY YSFNKMITPT IIKE
