AC   PRU00892;
DC   Domain;
TR   PROSITE; PS51559; SAM_RMT2; 1; level=0
XX
Names: Arginine and arginine-like N-methyltransferase.
Function: Guanidinoacetate N-methyltransferase (EC 2.1.1.2) is an enzyme that
 transfers a methyl group from S-adenosyl-L-methionine (SAM) to
 guanidinoacetate to form creatine and S-adenosyl-L-homocysteine.
XX
case <OC:Chordata> and <Length>=210> and <Length<=280>
DE   + RecName: EC=2.1.1.2;
else
DE   + RecName: EC=2.1.1.-;
end case
XX
case <OC:Chordata> and <Length>=210> and <Length<=280>
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;
end case
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RMT2 methyltransferase family.
XX
case <OC:Chordata> and <Length>=210> and <Length<=280>
GO   GO:0030731; F:guanidinoacetate N-methyltransferase activity
else case (<OC:Fungi> or <OC:Viridiplantae>) and <Length>=315> and <Length<=540>
GO   GO:0019702; F:protein arginine N5-methyltransferase activity
else
GO   GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity
end case
GO   GO:0032259; P:methylation
GO   GO:0046500; P:S-adenosylmethionine metabolic process
XX
KW   Methyltransferase
KW   S-adenosyl-L-methionine
KW   Transferase
XX
FT   From: PS51559
FT   DOMAIN          from..to
FT                   /note="RMT2 #"
FT   BINDING         69..74
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   Condition: [FH]-G-[LM]-[AGS]-[IL]-[AFISV]
FT   REGION          90..92
FT                   /note="S-adenosyl-L-methionine"
FT   Condition: E-[ACP]-[HN]
FT   BINDING         117..118
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   Condition: W-[EQ]
case <OC:Chordata> and <Length>=210> and <Length<=280>
FT   BINDING         169..170
FT                   /ligand="guanidinoacetate"
FT                   /ligand_id="ChEBI:CHEBI:57742"
FT   Condition: L-T
end case
FT   BINDING         20
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   Condition: [FWY]
case <OC:Chordata> and <Length>=210> and <Length<=280>
FT   BINDING         41
FT                   /ligand="guanidinoacetate"
FT                   /ligand_id="ChEBI:CHEBI:57742"
FT   Condition: M
FT   BINDING         45
FT                   /ligand="guanidinoacetate"
FT                   /ligand_id="ChEBI:CHEBI:57742"
FT   Condition: E
end case
FT   BINDING         49
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   Condition: [MS]
case <OC:Chordata> and <Length>=210> and <Length<=280>
FT   BINDING         137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   Condition: D
FT   BINDING         137
FT                   /ligand="guanidinoacetate"
FT                   /ligand_id="ChEBI:CHEBI:57742"
FT   Condition: D
else
FT   BINDING         137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   Condition: D
end case
XX
Chop: Nter=0; Cter=0;
Size: unlimited;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P10868;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.20 2022/11/19
//