ID   GSH1_YERPS              Reviewed;         519 AA.
AC   Q66E64;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Glutamate--cysteine ligase {ECO:0000255|HAMAP-Rule:MF_00578};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_00578};
DE   AltName: Full=Gamma-ECS {ECO:0000255|HAMAP-Rule:MF_00578};
DE            Short=GCS {ECO:0000255|HAMAP-Rule:MF_00578};
DE   AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000255|HAMAP-Rule:MF_00578};
GN   Name=gshA {ECO:0000255|HAMAP-Rule:MF_00578}; OrderedLocusNames=YPTB0829;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-
CC         cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00578};
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC       L-cysteine and L-glutamate: step 1/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00578}.
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 1 family.
CC       Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00578}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX936398; CAH20069.1; -; Genomic_DNA.
DR   RefSeq; WP_011191809.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66E64; -.
DR   SMR; Q66E64; -.
DR   EnsemblBacteria; CAH20069; CAH20069; YPTB0829.
DR   KEGG; ypo:BZ17_1722; -.
DR   KEGG; yps:YPTB0829; -.
DR   PATRIC; fig|273123.14.peg.1828; -.
DR   OMA; RYSWLLM; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000001011; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00578; Glu_cys_ligase; 1.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR007370; Glu_cys_ligase.
DR   InterPro; IPR006334; Glut_cys_ligase.
DR   PANTHER; PTHR38761; PTHR38761; 1.
DR   Pfam; PF04262; Glu_cys_ligase; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   TIGRFAMs; TIGR01434; glu_cys_ligase; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glutathione biosynthesis; Ligase; Nucleotide-binding.
FT   CHAIN           1..519
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_0000192548"
SQ   SEQUENCE   519 AA;  58497 MW;  2E839BF1345886B8 CRC64;
     MIPDVSHALT WLEAHPKALK GIRRGIERET LRVTADGHLA STGHPESLGA ALTHQWITTD
     FAEALLEFIT PVDGDIDHLL TFLRDIHRYT ARKLGDERMW PLSMPCFIEA EQDIELAKYG
     SSNIGRFKTL YREGLKNRYG ALMQTISGVH YNFSLPLEFW QAWAGVTDEQ SGKEEISAGY
     FRLIRNYYRF GWVIPYLFGA SPAICSSFLQ GRETALPFER NGKGMCYLPY ATSLRLSDLG
     YTNKSQSNLG ITFNDLHTYV DALKRAIQTP SEEYVALGLK DGDRHLQLNT NVLQIENELY
     APIRPKRVTR AGESPSDALL RGGIEYIEVR SLDINPFSPI GVDAVQARFL DLFLIWCVLA
     DAPEMSSDEL LCTRKNWDRV ILEGRKPGQT IGIGCSDSRQ PLETVGKALF ADLRRVAEVL
     DGSESASYQQ VCDELVASFD DPELTFSARI LKVMQEKGIG GVGLELAEHY REMLQNEPLE
     LLTEEQLSAE RDASRQRQHE LELKDKLSFE EYLALHGGQ