EGTD_MYCTU
ID EGTD_MYCTU Reviewed; 321 AA.
AC P9WN47; L0TG93; O69669; Q7D514;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Histidine N-alpha-methyltransferase;
DE EC=2.1.1.44 {ECO:0000250|UniProtKB:A0R5M8};
DE AltName: Full=Histidine trimethyltransferase;
GN Name=egtD; OrderedLocusNames=Rv3701c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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:0000250|UniProtKB:A0R5M8}.
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 Evidence={ECO:0000250|UniProtKB:A0R5M8};
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000250|UniProtKB:A0R5M8}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:A0R5M8}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. EgtD family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP46526.1; -; Genomic_DNA.
DR PIR; F70793; F70793.
DR RefSeq; NP_218218.1; NC_000962.3.
DR RefSeq; WP_003419799.1; NZ_NVQJ01000028.1.
DR AlphaFoldDB; P9WN47; -.
DR SMR; P9WN47; -.
DR STRING; 83332.Rv3701c; -.
DR PaxDb; P9WN47; -.
DR DNASU; 885521; -.
DR GeneID; 885521; -.
DR KEGG; mtu:Rv3701c; -.
DR TubercuList; Rv3701c; -.
DR eggNOG; COG4301; Bacteria.
DR OMA; RVEMHLV; -.
DR PhylomeDB; P9WN47; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0030745; F:dimethylhistidine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008276; F:protein methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0052704; P:ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide; ISS:UniProtKB.
DR GO; GO:0052707; P:N-alpha,N-alpha,N-alpha-trimethyl-L-histidine biosynthesis from histidine; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 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 Pfam; PF10017; Methyltransf_33; 1.
DR PIRSF; PIRSF018005; UCP018005; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR03438; egtD_ergothio; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..321
FT /note="Histidine N-alpha-methyltransferase"
FT /id="PRO_0000413652"
FT BINDING 56
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:A0R5M8"
FT BINDING 86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A0R5M8"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A0R5M8"
FT BINDING 113
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A0R5M8"
FT BINDING 141..142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A0R5M8"
FT BINDING 166
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:A0R5M8"
FT BINDING 206
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:A0R5M8"
FT BINDING 282..284
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:A0R5M8"
SQ SEQUENCE 321 AA; 35404 MW; 28FE9989B22A9D77 CRC64;
MRVSVANHLG EDAGHLALRR DVYSGLQKTP KSLPPKWFYD TVGSELFDQI TRLPEYYPTR
AEAEILRARS AEVASACRAD TLVELGSGTS EKTRMLLDAL RHRGSLRRFV PFDVDASVLS
ATATAIQREY SGVEINAVCG DFEEHLTEIP RGGRRLFVFL GSTIGNLTPG PRAQFLTALA
GVMRPGDSLL LGTDLVKDAA RLVRAYDDPG GVTAQFNRNV LAVINRELEA DFDVDAFQHV
ARWNSAEERI EMWLRADGRQ RVRVGALDLT VDFDAGEEML TEVSCKFRPQ AVGAELAAAG
LHRIRWWTDE AGDFGLSLAA K
