ID   GSH1_PSEPK              Reviewed;         525 AA.
AC   Q88R90;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=PP_0243;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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}.
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DR   EMBL; AE015451; AAN65875.1; -; Genomic_DNA.
DR   RefSeq; NP_742411.1; NC_002947.4.
DR   AlphaFoldDB; Q88R90; -.
DR   SMR; Q88R90; -.
DR   STRING; 160488.PP_0243; -.
DR   EnsemblBacteria; AAN65875; AAN65875; PP_0243.
DR   KEGG; ppu:PP_0243; -.
DR   PATRIC; fig|160488.4.peg.259; -.
DR   eggNOG; COG2918; Bacteria.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   PhylomeDB; Q88R90; -.
DR   BioCyc; PPUT160488:G1G01-265-MON; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000000556; 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;
KW   Reference proteome.
FT   CHAIN           1..525
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_0000192533"
SQ   SEQUENCE   525 AA;  59068 MW;  F868F5EC025D580B CRC64;
     MSELLNRRLS LLGANLPLLK QCLHGIEREC LRVTDEGRLA QTPHPEALGS ALTNEQITTD
     YSESLLEFIT PALADPAKVL ESLEETHRFV YSKLGDEYLW SPSMPCTLPA EEDIPIAEYG
     SSNIGKLKHV YRKGLALRYG RTMQCIAGIH YNFSLPEALW PLLREAEGST ENDRDYQSSA
     YIALIRNFRR YSWLLMYLFG ASPALDKGFL RGRPHQLEEL DAETLFLPYA TSLRMSDLGY
     QSNAQAGLTP CYNNLASYTD SLRKAVGTPY PPYVEIGTHV DGEWVQLNTN ILQIENEYYS
     NIRPKRVTYT GERPIQALTS RGVQYVEVRC LDINPFLPVG IDLTEARFLD AFLLFCALED
     SPQLDNGECG QCTSNFLTVV KEGRRPGLEL HRNGQPISLK DWASELIGRI RQLANLLDQA
     QGSDEHAKAL DAQQAKVDDT SLTPSAQVLA RMTEHDESFV QFSLRQSRVH AETFREQPLS
     NEKQQAFETL ARESLARQSE LEQNEVGDFD LFVGAYQASI LAISS