ID   GSH1_SHEHH              Reviewed;         522 AA.
AC   B0TK23;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=Shal_1241;
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=458817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000931; ABZ75810.1; -; Genomic_DNA.
DR   RefSeq; WP_012276351.1; NC_010334.1.
DR   AlphaFoldDB; B0TK23; -.
DR   SMR; B0TK23; -.
DR   STRING; 458817.Shal_1241; -.
DR   EnsemblBacteria; ABZ75810; ABZ75810; Shal_1241.
DR   KEGG; shl:Shal_1241; -.
DR   eggNOG; COG2918; Bacteria.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   OrthoDB; 967793at2; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000001317; 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..522
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_1000082361"
SQ   SEQUENCE   522 AA;  58583 MW;  3290C86DBCB7ECA7 CRC64;
     MKPFNELVGK LSDAASRQAL KSMHRGIERE ALRIEKSGHL ALDKHPKALG SALMHSRITT
     DYSESLLEFI TPVFEDIDEL VEDLTLTHAY SVRHLNGQRL WPVSMPCYLG DAGDIPIADY
     GSSNTGQMKR LYRKGLTYRY GAQMQIISGV HFNFSVSDQL WNRLYELSDT SLSLEEFISE
     SYFGLIRNYR RLVWVLPYLF GASPALCSTF IQDPKTNEFP FEVIGNGTLY LPYATSLRMS
     DLGYTNQEQD NLNISYNSLA CYLEGMKSAI NMPSAKFAKI GVKVDGEYRQ LNANILQIEN
     EFYSPIRAKR VAKGNEKPSE SLARAGVEYI EVRALDVNPY SAVGIEKSQI RFLDLFLLNC
     LLQPSPASDA SEEAEIAANL QAVVLEGRKP GLKLTRAGEE VSLSGWLESL FGNLNDIAKL
     LDDEGQDDYQ VALAKWQKAV NDPDATLSGQ IIKGLKDNQI DHGDWVLQLA EQYHQELKGY
     PLSEAVTMRY EQDAQASLEK QARLEAEPSV SFDDFLADYF KA