ID D6Z7A9_SEGRD Unreviewed; 325 AA.
AC D6Z7A9;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=Srot_1375 {ECO:0000313|EMBL:ADG97839.1};
OS Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM
OS 44985 / JCM 13578).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Segniliparaceae;
OC Segniliparus.
OX NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG97839.1, ECO:0000313|Proteomes:UP000002247};
RN [1] {ECO:0000313|EMBL:ADG97839.1, ECO:0000313|Proteomes:UP000002247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC {ECO:0000313|Proteomes:UP000002247};
RX PubMed=21304703; DOI=10.4056/sigs.791633;
RA Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M., Schneider S.,
RA Bruce D., Goodwin L., Pitluck S., Liolios K., Mikhailova N., Pati A.,
RA Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chertkov O., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Detter J.C., Han C.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT 1076).";
RL Stand. Genomic Sci. 2:203-211(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; CP001958; ADG97839.1; -; Genomic_DNA.
DR AlphaFoldDB; D6Z7A9; -.
DR STRING; 640132.Srot_1375; -.
DR KEGG; srt:Srot_1375; -.
DR eggNOG; COG4301; Bacteria.
DR HOGENOM; CLU_049766_1_0_11; -.
DR OrthoDB; 5289726at2; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000002247; 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; 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:UP000002247};
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 25..323
FT /note="Histidine-specific methyltransferase SAM-dependent"
FT /evidence="ECO:0000259|Pfam:PF10017"
FT BINDING 63
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
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 99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 144..145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 169
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 209
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 285..287
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
SQ SEQUENCE 325 AA; 36300 MW; 1AEC53E0976D2427 CRC64;
MTPLDTGPLS TRTQLLQEDD LRRGLREDVL AGLRATPKRL APKWLYDAAG SELFDAITAL
PEYYPTEAER AALRLAADEI AERSGARTVM ELGSGSSDKT RTILDALRPH RYIAFDVSES
ALDGAAAGLR RRYPGMRVDC VVGDFDQHLA FLPEGADRML VFLGGTIGNY PPEPRAKLLS
AMSATLQPGE TLLLGTDLVK DPRRLVRAYD DSAGVTAAFN RNILTILNRE LRADFDLDGF
EHVALWDTDN EWIEMRLRAR RAQHVRVAEL DLDVDFAEGE EMHTEVSCKF RREKVEQELD
GAGLDLIGWW TDPAEDFGLS LSRKR
//
