ID   GSH1_SALPA              Reviewed;         518 AA.
AC   Q5PF10;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Glutamate--cysteine ligase;
DE            EC=6.3.2.2;
DE   AltName: Full=Gamma-glutamylcysteine synthetase;
DE   AltName: Full=Gamma-ECS;
DE            Short=GCS;
GN   Name=gshA; OrderedLocusNames=SPA2677;
OS   Salmonella paratyphi A.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=54388;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P.,
RA   Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M.,
RA   Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G.,
RA   Kohlberg S., Strong C., Du F., Carter J., Kremizki C., Layman D.,
RA   Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P.,
RA   Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L.,
RA   Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + L-cysteine = ADP +
CC       phosphate + gamma-L-glutamyl-L-cysteine.
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
CC       from L-cysteine and L-glutamate: step 1/2.
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 1
CC       family. Type 1 subfamily.
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DR   EMBL; CP000026; AAV78538.1; -; Genomic_DNA.
DR   RefSeq; YP_151850.1; -.
DR   SMR; Q5PF10; 1-514.
DR   GeneID; 3177337; -.
DR   GenomeReviews; CP000026_GR; SPA2677.
DR   KEGG; spt:SPA2677; -.
DR   HOGENOM; Q5PF10; -.
DR   OMA; Q5PF10; EYIEVRA.
DR   BioCyc; SENT295319:SPA2677-MON; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:HAMAP.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00578; -; 1.
DR   InterPro; IPR007370; Glu_cys_ligase.
DR   InterPro; IPR006334; Glut_cys_ligase.
DR   Pfam; PF04262; Glu_cys_ligase; 1.
DR   TIGRFAMs; TIGR01434; glu_cys_ligase; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Glutathione biosynthesis; Ligase;
KW   Nucleotide-binding.
FT   CHAIN         1    518       Glutamate--cysteine ligase.
FT                                /FTId=PRO_0000192537.
SQ   SEQUENCE   518 AA;  58384 MW;  9766882B28965C47 CRC64;
     MIPDVSQALA WLEKHPQALK GIQRGLERET LRVNADGTLA TTGHPEALGS ALTHKWITTD
     FAEALLEFIT PVDGDIQHML TFMRDLHRYT ARKLGDERMW PLSMPCYIAE GQDIELAQYG
     TSNTGRFKTL YREGLKNRYG ALMQTISGVH YNFSLPMAFW QAKCGVTEGE AAKEKISAGY
     FRLIRNYYRF GWVIPYLFGA SPAICSSFLQ GKPTTLPFEK TDCGMYYLPY ATSLRLSDLG
     YTNKSQSNLG ITFNDLHEYV AGLKRAIKTP SEEYARIGVE KDGKRLQINS NVLQIENELY
     APIRPKRVTR SGESPSDALL RGGIEYIEVR SLDINPFSPI GVDEQQVRFL DLFMVWCVLA
     DAPEMSSDEL LCTRTNWNRV ILEGRKPGLT LGIGCETAQF PLPKVGKDLF RDLKRVAQTL
     DSIHGGEEYQ KVCDELVACF DNPELTFSAR ILRSMIDEGI GGTGKAFGEA YRNLLREEPL
     EILQEEEFIA ERDASVRRQQ EIEAADTEPF AAWLAKHA
//