ID   GSH1_BUCAI              Reviewed;         518 AA.
AC   P57485;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-MAY-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=BU407;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB13108.1; -; Genomic_DNA.
DR   RefSeq; NP_240222.1; NC_002528.1.
DR   RefSeq; WP_010896101.1; NC_002528.1.
DR   AlphaFoldDB; P57485; -.
DR   SMR; P57485; -.
DR   STRING; 107806.10039074; -.
DR   EnsemblBacteria; BAB13108; BAB13108; BAB13108.
DR   KEGG; buc:BU407; -.
DR   PATRIC; fig|107806.10.peg.419; -.
DR   eggNOG; COG2918; Bacteria.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000001806; 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..518
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_0000192520"
SQ   SEQUENCE   518 AA;  60979 MW;  AC6659F1E2C50BD4 CRC64;
     MIEDISKKIA WLKKNPKMLK GIFRGIERET LRIQKNGHFS KTIHPYLIGS SLTHKWITTD
     FSENLLEFIT PTSDNIDYLL SFLTDLHSFT ASKIKNERMW PFSIPYCFND QTNIQIAQYG
     KSNIGKMKTT YRIGLKNRYG DLINTISGIH YNFSLPLFFW TNWENNQNKK NNTDLISSGY
     LNLIRNYYRF GWIVPYLFGS SPAISSFFLK NTKKKYKFKK NKEDIFYLPW STSLRLSDIG
     YSNTNILDLN IMFNDFNEYI ESFQNALKTP SKKFINIGLK DEHGNFKQLN TNILQIENEL
     YTQIRPKRKT KDGESLLEAL KNRGIEYVEI RSLDVNPFSP IGINKNQILL LDLFLIWCAL
     IDSPKIDKTD FLLTTKNWER IIYEGRKPNQ KIYINNNNET KTLIEIGQII FKDLNEIALI
     LDSNSNDLLY QKACKETQLF LKNPELTYSA QCLNFLMTTG IKKTGLYLAN KYHEKFINKN
     YFNLNQSVLE QEVIRSHQKK IEIEREDILS FEEYIRNK