ID A0A1X0UTJ1_9NOCA Unreviewed; 324 AA.
AC A0A1X0UTJ1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=BJI47_08330 {ECO:0000313|EMBL:ORI27088.1};
OS Rhodococcus sp. 1168.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=2018041 {ECO:0000313|EMBL:ORI27088.1, ECO:0000313|Proteomes:UP000192546};
RN [1] {ECO:0000313|EMBL:ORI27088.1, ECO:0000313|Proteomes:UP000192546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1168 {ECO:0000313|EMBL:ORI27088.1,
RC ECO:0000313|Proteomes:UP000192546};
RA Nahar A.;
RT "Metabolic and lipid synthesis pathways analysis of sub-Antarctic
RT Rhodococcus luteus.";
RL Submitted (OCT-2016) 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:ORI27088.1}.
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DR EMBL; MKKY01000020; ORI27088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0UTJ1; -.
DR OrthoDB; 5289726at2; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000192546; 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 GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
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:UP000192546};
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..321
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 114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 142..143
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 167
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 207
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 283..285
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
SQ SEQUENCE 324 AA; 35680 MW; 999B7902A56B70EE CRC64;
MSDSALDVHI SPERLLEDLR SDVRQGLTAS PKWLSPKWFY DATGSELFER ITELPEYYPT
RTERALIEAH AYDIAERTDA AILVELGSGS SEKTRLLIEA GIKHGSLAKY VPQDVSPSAL
SGAIEQISHE FPALEVHGIV SDFTDTLQNL PADGRRTIAF LGGTLGNLIP EERAGFLSDI
AGALIPDEFL VLGVGLVIDP DVLIPAYDDA AGVTAEFNVN VLSVLNDRLG ANFDRSQFDH
VAVWDADNEW IEMRLRARSA QQVAIGDLDL DIEFAEGEEV RTEISAKFRR EGITAELADA
GFGVDQFWTD PQERFALILA RRGR
//
