ID   GSH1_ALIF1              Reviewed;         521 AA.
AC   Q5E7F8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=VF_0543;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW85038.1; -; Genomic_DNA.
DR   RefSeq; WP_011261306.1; NC_006840.2.
DR   RefSeq; YP_203926.1; NC_006840.2.
DR   AlphaFoldDB; Q5E7F8; -.
DR   SMR; Q5E7F8; -.
DR   STRING; 312309.VF_0543; -.
DR   EnsemblBacteria; AAW85038; AAW85038; VF_0543.
DR   KEGG; vfi:VF_0543; -.
DR   PATRIC; fig|312309.11.peg.536; -.
DR   eggNOG; COG2918; Bacteria.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   OrthoDB; 967793at2; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000000537; Chromosome I.
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..521
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_0000192542"
SQ   SEQUENCE   521 AA;  59405 MW;  6756B4B04DCFA22A CRC64;
     MTEFINRLQK VASNPNAFKK TGRGIERETL RFTLGASLST KPHPEGVGSA LTHKYITTDF
     AESLLEFITP VSNDVDTVLK QLEDVHHYTV SHMGDEKLWP LSMPCFVTHD DDITLAQYGE
     SNVGKLKTTY REGLKRRYGS VMQVISGVHF NFSFSTEFWD ELFGEQSEDQ RKESVSDAYF
     ALIRNYYRFG WLIPYFFGAS PALCSSFIQG RETSMDFESL GKTYYLPYAT SLRLSDLGYT
     NDAQSNLKIS LNSVNEYVDG LNKAIRTPSE EFAKIGLKEG DKHIQLNSNV LQIENELYAP
     IRPKRVTKSG ERPSEALERD GVEYIEVRSL DVNPYSPIGV NEDQVRFLDM FLTWTVLSDS
     APMNDSEMAC WKDNWNKIIE KGRKPGLELK IGCQGERLTQ KAWAERVFED LLVIAKEMDR
     VNGDDAYQQT HKRLSAMIDD PELTISGRLL AETKAAGGIG VIGCKLAVEH RETHLAHQYR
     FYTKQELDAE VERSVQAQKE IEANDKLSFS EYLEEYFSYL K