(data stored in ACNUC7421 zone)

SWISSPROT: B1VRV9_STRGG

ID   B1VRV9_STRGG            Unreviewed;       320 AA.
AC   B1VRV9;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 49.
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=SGR_698 {ECO:0000313|EMBL:BAG17527.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG17527.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG17527.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism
RT   Streptomyces griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
CC   -!- FUNCTION: Catalyzes the SAM-dependent triple methylation of the
CC       alpha-amino group of histidine to form hercynine, a step in the
CC       biosynthesis pathway of ergothioneine. {ECO:0000256|HAMAP-
CC       Rule:MF_02037}.
CC   -!- CATALYTIC ACTIVITY: 3 S-adenosyl-L-methionine + L-histidine = 3 S-
CC       adenosyl-L-homocysteine + hercynine. {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
CC       family. {ECO:0000256|HAMAP-Rule:MF_02037}.
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DR   EMBL; AP009493; BAG17527.1; -; Genomic_DNA.
DR   RefSeq; WP_012377997.1; NC_010572.1.
DR   STRING; 455632.SGR_698; -.
DR   EnsemblBacteria; BAG17527; BAG17527; SGR_698.
DR   GeneID; 6213680; -.
DR   KEGG; sgr:SGR_698; -.
DR   PATRIC; fig|455632.4.peg.679; -.
DR   eggNOG; ENOG41067HS; Bacteria.
DR   eggNOG; COG4301; LUCA.
DR   HOGENOM; HOG000253490; -.
DR   KO; K18911; -.
DR   OMA; RVEMHLV; -.
DR   UniPathway; UPA01014; -.
DR   Proteomes; UP000001685; Chromosome.
DR   GO; GO:0030745; F:dimethylhistidine N-methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro.
DR   GO; GO:0052699; P:ergothioneine biosynthetic process; IEA:UniProtKB-HAMAP.
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.
DR   Pfam; PF10017; Methyltransf_33; 1.
DR   PIRSF; PIRSF018005; UCP018005; 1.
DR   SUPFAM; SSF53335; SSF53335; 2.
DR   TIGRFAMs; TIGR03438; egtD_ergothio; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1VRV9.
DR   SWISS-2DPAGE; B1VRV9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001685};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_02037};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001685};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_02037};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02037}.
FT   DOMAIN       19    318       Methyltransf_33. {ECO:0000259|Pfam:
FT                                PF10017}.
FT   REGION      139    140       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_02037}.
FT   REGION      280    282       L-histidine binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_02037}.
FT   BINDING      57     57       L-histidine. {ECO:0000256|HAMAP-Rule:
FT                                MF_02037}.
FT   BINDING      87     87       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02037}.
FT   BINDING      93     93       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02037}.
FT   BINDING     111    111       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02037}.
FT   BINDING     164    164       L-histidine. {ECO:0000256|HAMAP-Rule:
FT                                MF_02037}.
FT   BINDING     204    204       L-histidine. {ECO:0000256|HAMAP-Rule:
FT                                MF_02037}.
SQ   SEQUENCE   320 AA;  34972 MW;  18CD217F4AE537C4 CRC64;
     MSPFLLTRTL PVDATGAALR ADVLSGLTRH PKTLPPKWFY DARGSELFEE ITRLPEYYPT
     RAEREILQAR AEEIAAASGA RTVIELGSGS SEKTRHLLDV LPELHSYVPV DVSESALTGA
     AESLLVEHPG LSVHALIADF TGGLALPGTP GPRLVVFLGG TIGNLLPEER AGFLRSVRSL
     LSPGDALLLG TDLVKDEETL VAAYDDAAGV TAAFNKNVLS VVNRELGADF PLDDFDHLAV
     WNPRDRWIEM RLRARRALNV KIRELDLVVP FEAGEELRTE VSAKFRREDV REELAAAGMR
     LTQWWTDSAG RFALSLATAV
//

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