ID A0A2A3GUK8_9ACTN Unreviewed; 323 AA.
AC A0A2A3GUK8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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=BKI49_32755 {ECO:0000313|EMBL:PBC59784.1};
OS Streptomyces sp. Tue6028.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2036037 {ECO:0000313|EMBL:PBC59784.1, ECO:0000313|Proteomes:UP000217789};
RN [1] {ECO:0000313|EMBL:PBC59784.1, ECO:0000313|Proteomes:UP000217789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tue6028 {ECO:0000313|EMBL:PBC59784.1,
RC ECO:0000313|Proteomes:UP000217789};
RA Greule A., Flemming S., Bechthold A.;
RT "The Draft Genome Sequence of Streptomyces sp. Tue6028 - Producer of
RT Polyketomycin and Foxicin.";
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:PBC59784.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MLCE01000036; PBC59784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3GUK8; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000217789; 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; 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:UP000217789};
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..316
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 323 AA; 34775 MW; 78341BE43A7D94D7 CRC64;
MSPFLLTRTL PEDATDAALR ADVLHGLTGT PKTLPPKWFY DAHGSELFEK ITELPEYYPT
RAEREILLAR AGEIALASGA RTLVELGSGS SEKTRHLLDA LPGLHTYVPV DVSESALTQA
GQALAAERPG LDVHALIADF TGSLTLPDTP GPRLVAFLGG TIGNLLPAER AAFLASVRAL
LSPGDALLLG TDLVKDESVL VAAYDDAAGV TAAFNKNVLS VVNRELEADF DPDAFDHVAL
WDTEQEWIEM RLRSRAAQTV KIPALDLAVH FARGEELRTE VSAKFREDGV RAELASAGFA
LTHWWTDAEG RFALSLSVAG QDR
//
