ID   GSH1_VIBVU              Reviewed;         525 AA.
AC   Q8DC38;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=VV1_1606;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) 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; AE016795; AAO10027.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8DC38; -.
DR   SMR; Q8DC38; -.
DR   EnsemblBacteria; AAO10027; AAO10027; VV1_1606.
DR   KEGG; vvu:VV1_1606; -.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000002275; Chromosome 1.
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..525
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_0000192544"
SQ   SEQUENCE   525 AA;  59632 MW;  1D122E70213FCFE1 CRC64;
     MNFILTDFAA RLELVARNPE VFKQFGRGVE RETLRYSQNG RIATTMHPQG LGSAFTNQWI
     TTDFAESLLE FITPVSHDID VLLGQLDDIH HFTQTQLGEE KMWPMSMPCY VETEDQITLA
     QYGSSNSAKM KTLYREGLKR RYGSLMQIIS GVHFNFSFPE SFWDALHGEQ TEDERQATKS
     EAYFGLIRNY YRFGWLIPYF FGASPAMCSS FLQGRETSLP FEALGKTLYL PKATSLRLSD
     LGYTNSAQSV LTIGFNSIDE YLEGLTKAIR TPSAEFAKLG VKENGEYRQL NSNVLQIENE
     LYAPIRPKRV AKNGEKPSEA LARGGVEYIE VRSLDVNPFT PVGITETQVR FLDLFLTWAA
     LSESQPMDQC ELACWRENWN KVVVSGREYG LELQIGCKGE KLSLQAWAHR VFAELRQLAE
     VMDSAHGDNQ YSLACSELEQ WIDHPEKTLS AQLLTLIQQN GSLGATGCEL GGAYREQNLA
     HHYRHFSLQQ MEQEVALSLI KQSQIEQADE VDFDTYLADY FAYLK