(data stored in ACNUC7421 zone)

SWISSPROT: B1VRV7_STRGG

ID   B1VRV7_STRGG            Unreviewed;       467 AA.
AC   B1VRV7;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   07-JUN-2017, entry version 57.
DE   RecName: Full=Hercynine oxygenase {ECO:0000256|HAMAP-Rule:MF_02035};
DE            EC=1.14.99.50 {ECO:0000256|HAMAP-Rule:MF_02035};
DE   AltName: Full=Gamma-glutamyl hercynylcysteine S-oxide synthase {ECO:0000256|HAMAP-Rule:MF_02035};
GN   Name=egtB {ECO:0000256|HAMAP-Rule:MF_02035};
GN   OrderedLocusNames=SGR_696 {ECO:0000313|EMBL:BAG17525.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG17525.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG17525.1, 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 oxidative sulfurization of hercynine (N-
CC       alpha,N-alpha,N-alpha-trimethyl-L-histidine) into hercynyl-gamma-
CC       L-glutamyl-L-cysteine sulfoxide, a step in the biosynthesis
CC       pathway of ergothioneine. {ECO:0000256|HAMAP-Rule:MF_02035}.
CC   -!- CATALYTIC ACTIVITY: Hercynine + gamma-L-glutamyl-L-cysteine + O(2)
CC       = gamma-L-glutamyl-S-hercyn-2-yl-L-cysteine S-oxide + H(2)O.
CC       {ECO:0000256|HAMAP-Rule:MF_02035}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02035};
CC   -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02035}.
CC   -!- SIMILARITY: Belongs to the EgtB family. {ECO:0000256|HAMAP-
CC       Rule:MF_02035}.
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DR   EMBL; AP009493; BAG17525.1; -; Genomic_DNA.
DR   ProteinModelPortal; B1VRV7; -.
DR   STRING; 455632.SGR_696; -.
DR   EnsemblBacteria; BAG17525; BAG17525; SGR_696.
DR   KEGG; sgr:SGR_696; -.
DR   eggNOG; ENOG4105E46; Bacteria.
DR   eggNOG; COG1262; LUCA.
DR   HOGENOM; HOG000253478; -.
DR   KO; K18912; -.
DR   OMA; YPHQRWQ; -.
DR   UniPathway; UPA01014; -.
DR   Proteomes; UP000001685; Chromosome.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProtKB-HAMAP.
DR   GO; GO:0052699; P:ergothioneine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_02035; EgtB; 1.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR024775; DinB-like.
DR   InterPro; IPR034660; DinB/YfiT-like.
DR   InterPro; IPR017806; EgtB.
DR   InterPro; IPR032890; EgtB_Actinobacteria.
DR   InterPro; IPR005532; SUMF_dom.
DR   Pfam; PF12867; DinB_2; 1.
DR   Pfam; PF03781; FGE-sulfatase; 1.
DR   SUPFAM; SSF109854; SSF109854; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   TIGRFAMs; TIGR03440; egtB_TIGR03440; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1VRV7.
DR   SWISS-2DPAGE; B1VRV7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001685};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_02035};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02035};
KW   Monooxygenase {ECO:0000256|HAMAP-Rule:MF_02035};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02035};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001685}.
FT   DOMAIN       47    179       DinB_2. {ECO:0000259|Pfam:PF12867}.
FT   DOMAIN      208    465       FGE-sulfatase. {ECO:0000259|Pfam:
FT                                PF03781}.
FT   REGION      117    120       Gamma-glutamylcysteine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_02035}.
FT   METAL        83     83       Iron; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02035}.
FT   METAL       171    171       Iron; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02035}.
FT   METAL       175    175       Iron; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02035}.
FT   BINDING     450    450       Gamma-glutamylcysteine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02035}.
FT   BINDING     454    454       Gamma-glutamylcysteine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02035}.
SQ   SEQUENCE   467 AA;  51850 MW;  B69589EE28549961 CRC64;
     MTDHREGTRH REHSDAFDPA GSTASTGFPV AAGIDPEALR RQALAALLSA RERTALLTDS
     VDDGELTAQH SPLMSPLVWD LAHIGNQEEQ WLLRAVGGRQ ALRPEIDGLY NAFEHSRASR
     PSLPLLAPAE ARTYASDVRG RALDLLEGVP LHEGGRPLER AGFAFGMIAQ HEQQHDETML
     ITHQLRSGPA ALTAPEPPAP VEAEVLGDEV LVPGGPFTMG TSAEPWALDN ERPAHRREVA
     AFHLDTSPVT CGAYLRFIED GGYGDSRWWA PEGWAMVREH DLTAPLFWRR EAGQWLRRRF
     GVTEPVPQDE PVLHVSWYEA DAYARWAGRR LPTESEWEKA ARHDPVSDRS RRYPWGDGDP
     TPERANLGQR HLRPARSGAY PAGRSPSGAG QLIGDVWEWT SSDFLPYPGF VAFPYREYSE
     VFFGPGHKVL RGGSFAVGEV ACRGTFRNWD LPVRRQIFSG FRTARSA
//

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