ID A0A3N1NHP5_9ACTN Unreviewed; 320 AA. AC A0A3N1NHP5; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 11-DEC-2019, entry version 5. DE RecName: Full=Histidine N-alpha-methyltransferase {ECO:0000256|HAMAP-Rule:MF_02037}; DE EC=2.1.1.44 {ECO:0000256|HAMAP-Rule:MF_02037}; DE AltName: Full=Histidine trimethyltransferase {ECO:0000256|HAMAP-Rule:MF_02037}; GN Name=egtD {ECO:0000256|HAMAP-Rule:MF_02037}; GN ORFNames=EDC83_7885 {ECO:0000313|EMBL:ROQ15339.1}; OS Streptomyces griseorubiginosus. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=67304 {ECO:0000313|EMBL:ROQ15339.1, ECO:0000313|Proteomes:UP000279460}; RN [1] {ECO:0000313|EMBL:ROQ15339.1, ECO:0000313|Proteomes:UP000279460} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAI-142 {ECO:0000313|EMBL:ROQ15339.1, RC ECO:0000313|Proteomes:UP000279460}; RA Coleman-Derr D.; RT "Genome sequencing of plant associated microbes to promote plant fitness in RT Sorghum bicolor and Oryza sativa."; RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000256|HAMAP-Rule:MF_02037}. 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_02037}; CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_02037}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02037}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. EgtD family. CC {ECO:0000256|HAMAP-Rule:MF_02037}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:ROQ15339.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; RJKZ01000001; ROQ15339.1; -; Genomic_DNA. DR UniPathway; UPA01014; -. DR Proteomes; UP000279460; Unassembled WGS sequence. DR GO; GO:0030745; F:dimethylhistidine N-methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro. DR GO; GO:0052699; P:ergothioneine biosynthetic process; IEA:UniProtKB-UniRule. DR HAMAP; MF_02037; EgtD; 1. DR InterPro; IPR035094; EgtD. DR InterPro; IPR032888; EgtD_Actinobacteria. DR InterPro; IPR019257; MeTrfase_dom. DR InterPro; IPR017804; MeTrfase_EgtD-like. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF10017; Methyltransf_33; 1. DR PIRSF; PIRSF018005; UCP018005; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR03438; egtD_ergothio; 1. PE 3: Inferred from homology; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_02037, KW ECO:0000313|EMBL:ROQ15339.1}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_02037}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_02037, ECO:0000313|EMBL:ROQ15339.1}. FT DOMAIN 19..317 FT /note="Methyltransf_33" FT /evidence="ECO:0000259|Pfam:PF10017" FT REGION 139..140 FT /note="S-adenosyl-L-methionine binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037" FT REGION 280..282 FT /note="L-histidine binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037" FT BINDING 57 FT /note="L-histidine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037" FT BINDING 87 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037" FT BINDING 93 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037" FT BINDING 111 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037" FT BINDING 164 FT /note="L-histidine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037" FT BINDING 204 FT /note="L-histidine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037" SQ SEQUENCE 320 AA; 34756 MW; 6E521C219FBDED0B CRC64; MTPFLLTRTL PEDATEAALR ADVLRGLTHT PKTLPPKWFY DAHGSELFEQ ITELPEYYPT RAEREILVAR SGEIAAATGA RTLVELGSGS SEKTRFLLDA LTGLHTYVPV DVSESALTQA GQALVAQRPE LSVHALIADF TAGLTLPGTP GPRLLAFLGG TIGNLLPAER ATFLSSVRAL LSPGDALLLG TDLVKDENVL VRAYDDAAGV TAAFNKNVLT VVNRELDADF DPGAFDHVAL WDAENEWIEM RLRSRTEQTV KVPALDLAVD FAAGEELYTE ISAKFRKEGV RDELSSAGLE LAHWWTDSEG RFALSLSVVR //