ID   GSH1_SHEPA              Reviewed;         522 AA.
AC   A8H1U8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=Spea_1208;
OS   Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=398579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700345 / ANG-SQ1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT   "Complete sequence of Shewanella pealeana ATCC 700345.";
RL   Submitted (OCT-2007) 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; CP000851; ABV86535.1; -; Genomic_DNA.
DR   RefSeq; WP_012154461.1; NC_009901.1.
DR   AlphaFoldDB; A8H1U8; -.
DR   SMR; A8H1U8; -.
DR   STRING; 398579.Spea_1208; -.
DR   EnsemblBacteria; ABV86535; ABV86535; Spea_1208.
DR   KEGG; spl:Spea_1208; -.
DR   eggNOG; COG2918; Bacteria.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000002608; 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..522
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_1000082362"
SQ   SEQUENCE   522 AA;  58929 MW;  8CB22838C92720AD CRC64;
     MKSFNELVGK LSDPASRQAL KSMQRGIERE ALRIEKSGHL ALDKHPKALG SALTHSRITT
     DYSESLLEFI TPVFADIDEL VEDLTLTHAY SVRHLNGQRL WPVSMPCYLG DGADIPIADY
     GSSNSGQMKS LYRKGLTYRY GAQMQIISGV HFNFSVSDKL WHRLYELSDK SLSLDDFISD
     SYFGLIRNYR RLVWVLPYLF GASPALCSTF IQDPKTSNFP FEVIGDGTLF MPYATSLRMS
     DLGYTNQEQD NLNISYNSLT DYLTGMQAAI NMPSANFAKI GVKVDGEYRQ LNDNILQIEN
     EFYSPIRAKR VAKGSEKPSE SLARAGVEYI EVRALDVNPY SAVGIEKSQI RFLDLFLLNC
     LLQPSAPSDA TEEAEIAENL QAVVLEGRKP GLLLKRSGQE LSLTHWLESL FGNLKQIAQL
     LDDEGQDDYQ VALAKWHKAV ENPNETLSGK IMAGLKDEQV DHSEWVMELA EQYHQQLKAY
     PLTENVDKRY QQDAVESLEK QAYLESQPSV SFDQFLVDYF KV