(data stored in SCRATCH zone)

SWISSPROT: B1VRV6_STRGG

ID   B1VRV6_STRGG            Unreviewed;       456 AA.
AC   B1VRV6;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   30-AUG-2017, entry version 50.
DE   RecName: Full=Glutamate--cysteine ligase EgtA {ECO:0000256|HAMAP-Rule:MF_02034};
DE            EC=6.3.2.2 {ECO:0000256|HAMAP-Rule:MF_02034};
DE   AltName: Full=Gamma-glutamylcysteine synthase {ECO:0000256|HAMAP-Rule:MF_02034};
DE            Short=GCS {ECO:0000256|HAMAP-Rule:MF_02034};
DE            Short=Gamma-ECS {ECO:0000256|HAMAP-Rule:MF_02034};
GN   Name=egtA {ECO:0000256|HAMAP-Rule:MF_02034};
GN   OrderedLocusNames=SGR_695 {ECO:0000313|EMBL:BAG17524.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG17524.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG17524.1, 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 synthesis of gamma-glutamylcysteine
CC       (gamma-GC). This compound is used as substrate for the
CC       biosynthesis of the low-molecular thiol compound ergothioneine.
CC       {ECO:0000256|HAMAP-Rule:MF_02034}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + L-cysteine = ADP +
CC       phosphate + gamma-L-glutamyl-L-cysteine. {ECO:0000256|HAMAP-
CC       Rule:MF_02034}.
CC   -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02034}.
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2
CC       family. EgtA subfamily. {ECO:0000256|HAMAP-Rule:MF_02034}.
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DR   EMBL; AP009493; BAG17524.1; -; Genomic_DNA.
DR   RefSeq; WP_012377994.1; NC_010572.1.
DR   ProteinModelPortal; B1VRV6; -.
DR   STRING; 455632.SGR_695; -.
DR   EnsemblBacteria; BAG17524; BAG17524; SGR_695.
DR   GeneID; 6215104; -.
DR   KEGG; sgr:SGR_695; -.
DR   PATRIC; fig|455632.4.peg.676; -.
DR   eggNOG; ENOG4105D1K; Bacteria.
DR   eggNOG; COG3572; LUCA.
DR   HOGENOM; HOG000068081; -.
DR   KO; K01919; -.
DR   OMA; FADWADG; -.
DR   UniPathway; UPA01014; -.
DR   Proteomes; UP000001685; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0052699; P:ergothioneine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_02034; EgtA; 1.
DR   InterPro; IPR017809; EgtA_Actinobacteria.
DR   InterPro; IPR035434; GCL_bact_plant.
DR   InterPro; IPR006336; GCS2.
DR   Pfam; PF04107; GCS2; 1.
DR   PIRSF; PIRSF017901; GCL; 1.
DR   TIGRFAMs; TIGR03444; EgtA_Cys_ligase; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1VRV6.
DR   SWISS-2DPAGE; B1VRV6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02034};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001685};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02034};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001685}.
SQ   SEQUENCE   456 AA;  48697 MW;  65802F77EA8E53C0 CRC64;
     MGWDISGANG SRPDAAPLDE SGAEDLLRGI CFKTGPPRTV GVELEWLIHD RERPDLPVGQ
     ERLDRAVEAV RALPLSAALT FEPGGQLELS SQPAGSLMEC VDTTAADLAA VRAALDTAGL
     APVGLGVDPW QAPLRRLREP RYEAMEAALD RTGPAGRAMM CTSASVQVCL DAGEEEPGPL
     GYGRRWQLAH LLGAVLVAAF ANSPFRQGRR TGWRSTRQSL WADLDPVRTL APGSGRAPRE
     AWAAHVLDTT VLCIRREEGP WEVPEGLTFR EWIRTGSPRP PVRADLDYHL TTLFPPVRPR
     GHLELRMIDA QSGPDGWLVP LAVATALFDD PEAAETVYRT LKPLAEASDA SAAPRNALWT
     TAAREGLADP ELRGAATACF GAALPALERM GASGAVRDTV AAFTDRYVAR GRCPADDLPE
     PGELSHRGLS SDQDLLSGPG PLSDHTPPRS GKAATA
//

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