AC MF_02037; DC Protein; auto TR HAMAP; MF_02037; -; 1; level=0 XX Names: EgtD XX ID EGTD DE RecName: Full=Histidine N-alpha-methyltransferase; DE EC=2.1.1.44; DE AltName: Full=Histidine trimethyltransferase; GN Name=egtD; XX CC -!- FUNCTION: Catalyzes the SAM-dependent triple methylation of the alpha- CC amino group of histidine to form hercynine, a step in the biosynthesis CC pathway of ergothioneine. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-histidine + 3 S-adenosyl-L-methionine = 3 H(+) + hercynine + CC 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:38471, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15781, ChEBI:CHEBI:57595, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789; EC=2.1.1.44; CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis. CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. EgtD family. XX DR Pfam; PF10017; Methyltransf_33; 1; trigger=no DR NCBIfam; TIGR03438; egtD_ergothio; 1; trigger=no DR PIRSF; PIRSF018005; UCP018005; 1; trigger=no XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX GO GO:0030745; F:dimethylhistidine N-methyltransferase activity GO GO:0052699; P:ergothioneine biosynthetic process XX FT From: EGTD_MYCS2 (A0R5M8) FT BINDING 141..142 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D-[FMLY] FT BINDING 282..284 FT /ligand="L-histidine" FT /ligand_id="ChEBI:CHEBI:57595" FT Optional; Condition: E-[VI]-S FT BINDING 56 FT /ligand="L-histidine" FT /ligand_id="ChEBI:CHEBI:57595" FT Condition: Y FT BINDING 86 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: G FT BINDING 92 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: K FT BINDING 113 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D FT BINDING 166 FT /ligand="L-histidine" FT /ligand_id="ChEBI:CHEBI:57595" FT Optional; Condition: N FT BINDING 206 FT /ligand="L-histidine" FT /ligand_id="ChEBI:CHEBI:57595" FT Optional; Condition: Y XX Size: 311-400; Related: None; Template: A0R5M8; Scope: Bacteria; Actinomycetota Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.8 2023/06/01 //