ID   GSH1_ERWT9              Reviewed;         519 AA.
AC   B2VHD0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, 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=ETA_26620;
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
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; CU468135; CAO97708.1; -; Genomic_DNA.
DR   RefSeq; WP_012442370.1; NC_010694.1.
DR   AlphaFoldDB; B2VHD0; -.
DR   SMR; B2VHD0; -.
DR   STRING; 465817.ETA_26620; -.
DR   EnsemblBacteria; CAO97708; CAO97708; ETA_26620.
DR   KEGG; eta:ETA_26620; -.
DR   eggNOG; COG2918; Bacteria.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   OrthoDB; 967793at2; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000001726; 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..519
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_1000129595"
SQ   SEQUENCE   519 AA;  58112 MW;  918E8B707B2FA7F8 CRC64;
     MIPDVSQALS WLEAHPDALN GIGRGIERET LRVRPDGYLA TTAHPTSLGA ALTHKWITTD
     FAEALLEFIT PVDRDIDRLL AFLRDIHRHT ARELGEERMW PMSMPCRVER DGDIELAQYG
     SSNIGQMKTL YRQGLKNRYG ALMQVISGVH YNFSLPLSFW QAWAGVNDAE SGKEAISAGY
     LRLIRNYYRF GWVIPYLFGA SPAICSSFLQ GKESKLPFEH GDNGMLSLPY ATSLRLSDLG
     YTNKSQSSLG IAFNNLPDYI SGLKAAIKTP SEEFAAMGVK DKNGDWLQLN TNVLQIENEL
     YAPIRPKRVT RSGEAPSDAL QRGGIEYIEV RSLDINPFSP IGVDADQVRF LDLFLIWCAL
     ADAPDMDSAE LACTRKNWNR VILEGRKPGQ TIGIGCGKTE RPLVDVGKAL FRDLLRVAKT
     LDSQGGECQY QEVCERLAAS FDDPDLTYSA RFLRTLQDNG IEKTGMALAE QYRAQLREEP
     LQVLTEQRFH DEAQRSRQSQ SEIEESDTLS LEAFLQGKS