ID C9Z4Y8_STRSW Unreviewed; 320 AA.
AC C9Z4Y8;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
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 OrderedLocusNames=SCAB_11241 {ECO:0000313|EMBL:CBG68292.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG68292.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG68292.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG68292.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
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}.
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DR EMBL; FN554889; CBG68292.1; -; Genomic_DNA.
DR RefSeq; WP_012999022.1; NC_013929.1.
DR AlphaFoldDB; C9Z4Y8; -.
DR STRING; 680198.SCAB_11241; -.
DR GeneID; 24309207; -.
DR KEGG; scb:SCAB_11241; -.
DR eggNOG; COG4301; Bacteria.
DR HOGENOM; CLU_049766_1_0_11; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000001444; Chromosome.
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 GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
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_sf.
DR NCBIfam; TIGR03438; egtD_ergothio; 1.
DR PANTHER; PTHR43397; ERGOTHIONEINE BIOSYNTHESIS PROTEIN 1; 1.
DR PANTHER; PTHR43397:SF1; ERGOTHIONEINE BIOSYNTHESIS PROTEIN 1; 1.
DR Pfam; PF10017; Methyltransf_33; 1.
DR PIRSF; PIRSF018005; UCP018005; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_02037}; Reference proteome {ECO:0000313|Proteomes:UP000001444};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_02037};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02037}.
FT DOMAIN 20..318
FT /note="Histidine-specific methyltransferase SAM-dependent"
FT /evidence="ECO:0000259|Pfam:PF10017"
FT BINDING 57
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 93
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 139..140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 164
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 204
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 280..282
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
SQ SEQUENCE 320 AA; 34559 MW; 1E3028B62C5B3C6A CRC64;
MSPFLLTRTL PEDATDAALR ADVLDGLTRT PKTLPPKWFY DARGSELFER ITELPEYYPT
RAEREILVGR AGEIAAASGA RTLVELGSGS SDKTRHLLDA MPGLHTYVPV DVSESALRQA
GEALVAERPG LNVHALIADF TAGLDLPGTP GPRLVVFLGG TIGNLVPAER AAFLAAVRAL
LAPGDALLLG TDLVKDEAVL VAAYDDAAGV TAEFNKNVLN VVDRELGADF DPDAFDHVAL
WNAECEWIEM RLRSRTAQTV KIPALDLAVD FEAGEELRTE VSAKFRREGV RAELASAGME
LTHWWTDEQG RFALSLSRAG
//
