ID   GSH1_BAUCH              Reviewed;         523 AA.
AC   Q1LTQ6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=BCI_0201;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H.,
RA   Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial symbiosis of
RT   sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
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; CP000238; ABF13792.1; -; Genomic_DNA.
DR   RefSeq; WP_011520391.1; NC_007984.1.
DR   AlphaFoldDB; Q1LTQ6; -.
DR   SMR; Q1LTQ6; -.
DR   STRING; 374463.BCI_0201; -.
DR   EnsemblBacteria; ABF13792; ABF13792; BCI_0201.
DR   KEGG; bci:BCI_0201; -.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   OrthoDB; 967793at2; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000002427; 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..523
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_1000025168"
SQ   SEQUENCE   523 AA;  60200 MW;  B91B940CE326C55B CRC64;
     MIPDVSSDTL FWLKANPQAL QGIYRGVERE TLRINTQGHL AQTPHPKKLG AALTHKWITT
     DFAETLLEFI TPVAQDIDHM LTLLRDIHRH VARHLCNEWM WPMSMPCFID SQQQIKLAQY
     GPSNMGRMKT LYRKGLKNRY SAMMQIISGV HYNFSLPLTF WQVYAGVSDM NSNKDIISAG
     YLGLIRNYYR FGWIIPYIFG ASPGVCQSFM KNRDTDLPFI KASSGFLYLP YATSLRMSDL
     GYANKSQSQL DITFNSLKEY VFRLKHAIRT PYADYQRIGL KKNGSYLQLN TNILQSENEL
     YAPIRPKRIT KNEESPLDAL LRRGIEYIEV RALDINPFSP VGIDEEQVRF LDLFLIWCTL
     APAPKMSTRE LLYTRLNWTK VILEGRKPGL TLIVDGGSSK KPLATIGKEL FSAMQALAET
     LDSHNGNIQY QQVCHKLRAC IDQPELTLSA RILKEMKKYG IRGLGLTLAN QYFQILLEEP
     LEMFNELTFD KEQIRSWHRQ LELEALDILS FDDFLAHINS HQQ