ID D2B0V4_STRRD Unreviewed; 326 AA.
AC D2B0V4;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
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=Sros_0329 {ECO:0000313|EMBL:ACZ83361.1};
OS Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI
OS 9100).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Streptosporangium.
OX NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ83361.1, ECO:0000313|Proteomes:UP000002029};
RN [1] {ECO:0000313|EMBL:ACZ83361.1, ECO:0000313|Proteomes:UP000002029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC {ECO:0000313|Proteomes:UP000002029};
RX PubMed=21304675; DOI=10.4056/sigs.631049;
RA Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., Glavina Del Rio T.,
RA Chen F., Tice H., Pitluck S., Cheng J.F., Chertkov O., Sims D., Meincke L.,
RA Brettin T., Han C., Detter J.C., Bruce D., Goodwin L., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Ivanova N., Mavromatis K., Mikhailova N.,
RA Chen A., Palaniappan K., Chain P., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Streptosporangium roseum type strain (NI
RT 9100).";
RL Stand. Genomic Sci. 2:29-37(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; CP001814; ACZ83361.1; -; Genomic_DNA.
DR RefSeq; WP_012887107.1; NC_013595.1.
DR AlphaFoldDB; D2B0V4; -.
DR STRING; 479432.Sros_0329; -.
DR KEGG; sro:Sros_0329; -.
DR eggNOG; COG4301; Bacteria.
DR HOGENOM; CLU_049766_1_0_11; -.
DR OrthoDB; 5289726at2; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000002029; 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:UP000002029};
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 24..325
FT /note="Histidine-specific methyltransferase SAM-dependent"
FT /evidence="ECO:0000259|Pfam:PF10017"
FT BINDING 61
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 91
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 97
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 146..147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 171
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 211
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
FT BINDING 287..289
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02037"
SQ SEQUENCE 326 AA; 35762 MW; D615487F8F08AF55 CRC64;
MSVSQSAVHL VNHLGHDYLR QALENDVRTG LTSTPKWLPP KWFYDAAGSD LFSQITRLPE
YYPTRRELAI LRREALDIAT RSGADTLVEL GSGTSEKTVL LLDALSSTGT LRTYTPVDVD
AVTLGDAARR LAARYPGLAV QAVCADFEHH LALLPREGRR MVAFLGGTIG NLDPAAREVF
LKELRGTLRS GDTFLLGADL VKDTGRLVAA YDDAAGVTAA FNRNVLHVVN RELDADFEPD
AFDHVAIYDA RQDWIEMRLR ASRAMRVRVG GLGLTVPFAA GEEMRTEISA KFRPEGLRKE
LAAAGFTVNH HYTDPTGDFS LVLARA
//
