ID   GSH1_BUCAP              Reviewed;         518 AA.
AC   P58994;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Glutamate--cysteine ligase;
DE            EC=6.3.2.2;
DE   AltName: Full=Gamma-ECS;
DE            Short=GCS;
DE   AltName: Full=Gamma-glutamylcysteine synthetase;
GN   Name=gshA; OrderedLocusNames=BUsg_392;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(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   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC       L-cysteine and L-glutamate: step 1/2.
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 1 family.
CC       Type 1 subfamily. {ECO:0000305}.
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DR   EMBL; AE013218; AAM67944.1; -; Genomic_DNA.
DR   RefSeq; WP_011053911.1; NC_004061.1.
DR   AlphaFoldDB; P58994; -.
DR   SMR; P58994; -.
DR   STRING; 198804.BUsg_392; -.
DR   EnsemblBacteria; AAM67944; AAM67944; BUsg_392.
DR   KEGG; bas:BUsg_392; -.
DR   eggNOG; COG2918; Bacteria.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   OrthoDB; 967793at2; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000000416; 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..518
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_0000192521"
SQ   SEQUENCE   518 AA;  61250 MW;  53E76B05654807F3 CRC64;
     MIEDISKKIS WLEKNPEIIK NIFRGIERET LRIKKNGKFS NTKHPYLLGS PLTHRWITTD
     FSENLLEFIT PTSSNIDYLI KFLKNLHSFV SYKIKHERMW PFSIPYLYNK STAIKIAEYG
     TSHLGKIKNI YRKGLKNRYG DLVNTISGIH YNFSLPKIFW KNWKKSEINL KNEDYISSGY
     LNLIRNYYRF GWVITYLFGA SPAISKYFLK DKKYKFKKNI ENILYLPWST SLRLSDIGYT
     KTPTIKLNIM FNDLKSYIKS LRKAINTPSK KFSKIGIKDK QGEFLQLNTN ILQMESELYT
     PIRPKRQTNP GESLLEALGK RGIEYIEIRS LDINPFSSIG INKKQILILD LFLIWCALIH
     APQMNKENFL VNNKNWNKII FEGRKPHQKI YINSQYETKT LIEIGQIIFQ DLKKIAKILD
     YQSKNFEYQK ACQETILFFK NPELTYSAKF LQLLIKHGIK KTGLNLANKY HKEFINRYNY
     NSEKNILERE TILSHKKQKQ IENNEISFKK NNFSHANN