ID   GSH1_VIBVY              Reviewed;         525 AA.
AC   Q7MHS5;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=VV2794;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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; BA000037; BAC95558.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7MHS5; -.
DR   SMR; Q7MHS5; -.
DR   STRING; 672.VV93_v1c25050; -.
DR   PRIDE; Q7MHS5; -.
DR   EnsemblBacteria; BAC95558; BAC95558; BAC95558.
DR   KEGG; vvy:VV2794; -.
DR   eggNOG; COG2918; Bacteria.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000002675; 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..525
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_0000192545"
SQ   SEQUENCE   525 AA;  59659 MW;  4CCCFF20315C34B7 CRC64;
     MNFILTDFAA RLELVARNPE VFKQFGRGVE RETLRYSQNG RIATSMHPQG LGSAFTNQWI
     TTDFAESLLE FITPVSHDID VLLGQLDDIH HFTQTQLGEE KMWPMSMPCY VETEDQITLA
     QYGSSNSAKM KTLYREGLKR RYGSLMQIIS GVHFNFSFPE SFWDALHGEQ TAEERQATKS
     EAYFGLIRNY YRFGWLIPYF FGASPAMCSS FLQGRETSLP FEALGKTLYL PKATSLRLSD
     LGYTNSAQSV LTIGFNSIDE YLEGLSKAIR TPSAEFAKLG VKENGEYRQL NSNVLQIENE
     LYAPIRPKRV AKNGEKPSEA LARGGVEYIE VRSLDVNPFT PVGITETQVR FLDLFLTWAA
     LSESQPMDQC ELACWRENWN KVVVSGREYG LELQIGCKGE KLSLQAWAHR VFAELRQLAE
     VMDSAHGDNQ YSLACSELEQ WIDHPEKTLS AQLLTLIQQN GSLGATGCEL GRAYREQNLA
     HHYRHFSLQQ MEQEVALSLI KQSQIEQADE VDFDTYLADY FAYLK