ID A0A3N1NHP5_9ACTN Unreviewed; 320 AA. AC A0A3N1NHP5; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 10-APR-2019, entry version 2. 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 RT fitness in 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 CC alpha-amino group of histidine to form hercynine, a step in the CC biosynthesis pathway of ergothioneine. {ECO:0000256|HAMAP- CC Rule:MF_02037}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-histidine + 3 S-adenosyl-L-methionine = 3 H(+) + CC hercynine + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:38471, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15781, ChEBI:CHEBI:57595, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.44; CC Evidence={ECO:0000256|HAMAP-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 CC family. {ECO:0000256|HAMAP-Rule:MF_02037}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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 Complete proteome {ECO:0000313|Proteomes:UP000279460}; 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, KW ECO:0000313|EMBL:ROQ15339.1}. FT DOMAIN 19 317 Methyltransf_33. {ECO:0000259|Pfam: FT PF10017}. FT REGION 139 140 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_02037}. FT REGION 280 282 L-histidine binding. {ECO:0000256|HAMAP- FT Rule:MF_02037}. FT BINDING 57 57 L-histidine. {ECO:0000256|HAMAP-Rule: FT MF_02037}. FT BINDING 87 87 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_02037}. FT BINDING 93 93 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_02037}. FT BINDING 111 111 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_02037}. FT BINDING 164 164 L-histidine. {ECO:0000256|HAMAP-Rule: FT MF_02037}. FT BINDING 204 204 L-histidine. {ECO:0000256|HAMAP-Rule: FT 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 //