ID   GSH1_PSESM              Reviewed;         529 AA.
AC   Q88AR1;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=PSPTO_0325;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO53870.1; -; Genomic_DNA.
DR   RefSeq; NP_790175.1; NC_004578.1.
DR   RefSeq; WP_005763456.1; NC_004578.1.
DR   AlphaFoldDB; Q88AR1; -.
DR   SMR; Q88AR1; -.
DR   STRING; 223283.PSPTO_0325; -.
DR   EnsemblBacteria; AAO53870; AAO53870; PSPTO_0325.
DR   GeneID; 1181934; -.
DR   KEGG; pst:PSPTO_0325; -.
DR   PATRIC; fig|223283.9.peg.341; -.
DR   eggNOG; COG2918; Bacteria.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   OrthoDB; 967793at2; -.
DR   PhylomeDB; Q88AR1; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000002515; 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..529
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_0000192534"
SQ   SEQUENCE   529 AA;  59495 MW;  CA3A6DBC708BC2FA CRC64;
     MSELLNRRLA LLGERNNLSL LEQCLHGIER ECLRVTPQAE LARTPHPQAL GAALTNGLVT
     TDYSESLLEF ITPALKNPVD TLDSLDKIHR FAYSKLDNEL LWSPSMPCPL PDEEHIPIAY
     YGTSNIGKLK YVYRKGLALR YGKTMQCIAG IHYNFSLPED AWALLKQTED FAGDARDYQS
     HSYIALIRNF RRYSWLLMYL FGASPALDAG FLRGREHQLE QFDADTLYLP YATSLRMSDL
     GYQSDAQADL TPCYNDLVSY TDSLRKAVAT PYKPYVDIGT HDQNGEWVQL NTNVLQIENE
     YYSNIRPKRV TYSGERPIQA LVARGVQYVE VRCLDINPFL PTGISLEQSR FIDAFVLYCA
     LEESQQLAGH ECSNASSNFL AVVKEGRRPG LNLQRDDSPV ELKAWATDLL EKITPIARLL
     DQAQGTDEHI KSIAVQQAKI DDTSLTPSAQ VLASMRAHGE GFTAFSLRQS QVHAEYFRTH
     PLSAAEQAHF EDLAKTSLEE QAELEATEEV VDFDTFVGSY QASILSISN