(data stored in SCRATCH zone)

SWISSPROT: B1VRV8_STRGG

ID   B1VRV8_STRGG            Unreviewed;       251 AA.
AC   B1VRV8;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   RecName: Full=Gamma-glutamyl-hercynylcysteine sulfoxide hydrolase {ECO:0000256|HAMAP-Rule:MF_02036};
DE            EC=3.5.1.118 {ECO:0000256|HAMAP-Rule:MF_02036};
DE   AltName: Full=Gamma-glutamyl hercynylcysteine S-oxide hydrolase {ECO:0000256|HAMAP-Rule:MF_02036};
GN   Name=egtC {ECO:0000256|HAMAP-Rule:MF_02036};
GN   OrderedLocusNames=SGR_697 {ECO:0000313|EMBL:BAG17526.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG17526.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG17526.1, 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 hydrolysis of the gamma-glutamyl amide
CC       bond of hercynyl-gamma-L-glutamyl-L-cysteine sulfoxide to produce
CC       hercynylcysteine sulfoxide, a step in the biosynthesis pathway of
CC       ergothioneine. {ECO:0000256|HAMAP-Rule:MF_02036}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-gamma-glutamyl-hercynylcysteine S-oxide = L-
CC         glutamate + S-(hercyn-2-yl)-L-cysteine S-oxide;
CC         Xref=Rhea:RHEA:42684, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:82703, ChEBI:CHEBI:82706; EC=3.5.1.118;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02036};
CC   -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02036}.
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DR   EMBL; AP009493; BAG17526.1; -; Genomic_DNA.
DR   RefSeq; WP_012377996.1; NC_010572.1.
DR   STRING; 455632.SGR_697; -.
DR   EnsemblBacteria; BAG17526; BAG17526; SGR_697.
DR   GeneID; 6214469; -.
DR   KEGG; sgr:SGR_697; -.
DR   PATRIC; fig|455632.4.peg.678; -.
DR   eggNOG; ENOG4108V75; Bacteria.
DR   eggNOG; COG0121; LUCA.
DR   HOGENOM; HOG000256686; -.
DR   KO; K07008; -.
DR   OMA; LFSHNGA; -.
DR   OrthoDB; 693464at2; -.
DR   BioCyc; SGRI455632:G1G2X-693-MONOMER; -.
DR   UniPathway; UPA01014; -.
DR   Proteomes; UP000001685; Chromosome.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProtKB-UniRule.
DR   GO; GO:0052699; P:ergothioneine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_02036; EgtC; 1.
DR   InterPro; IPR017808; EgtC.
DR   InterPro; IPR032889; EgtC_Actinobacteria.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR03442; TIGR03442; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1VRV8.
DR   SWISS-2DPAGE; B1VRV8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001685};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_02036};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_02036}.
FT   DOMAIN        2    251       Glutamine amidotransferase type-2.
FT                                {ECO:0000259|PROSITE:PS51278}.
SQ   SEQUENCE   251 AA;  26929 MW;  AB84A9680A51ACDF CRC64;
     MCRHIAYVGD PVALGEILLR PPHALVRQSW APRRQRHGTV NADGFGVGWY AEGDPVPGRY
     RRQGPIWGDE TFADLARVVR STALLAAVRD ATEAGADGEA AAAPYTAGRQ LFSHNGMVRG
     WPGSLADAAA ALPAERLLAL AARNDSALIW ALIRHRTDAG DDAPRAVAET VREVAAAAPG
     SRLNLLLTDG ETITATAWGD TLWYLTTPGR RTAVASEPYD DDPLWREVPD RTLLVATSTD
     VLLTPLKEPT A
//

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