ID   GSH1_PROMH              Reviewed;         526 AA.
AC   B4EUV9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=PMI0378;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM942759; CAR40970.1; -; Genomic_DNA.
DR   RefSeq; WP_004244777.1; NC_010554.1.
DR   AlphaFoldDB; B4EUV9; -.
DR   SMR; B4EUV9; -.
DR   STRING; 529507.PMI0378; -.
DR   EnsemblBacteria; CAR40970; CAR40970; PMI0378.
DR   GeneID; 6800192; -.
DR   KEGG; pmr:PMI0378; -.
DR   eggNOG; COG2918; Bacteria.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000008319; 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..526
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_1000129598"
SQ   SEQUENCE   526 AA;  59348 MW;  1DACC91A6978BE6D CRC64;
     MIPDVSKALS WLEAHPKVLC GIHRGIERET LRVTPDGHLA ATGHPVELGK SLTHKWITTD
     FAESLLEFIT PVDDNIDHTL HFLSDLHRYT ARHLTNERMW PMSMPCFIEA EDKITLAQFG
     TSNVGRFKTL YREGLKNRYG ALMQTISGVH YNFSLPIEFW QAWANITDEE TGKEAISDGY
     LRLIRNYYRF GWIIPFFFGA SPAICGSFLK GRKTNLPFEN TPKGAKYLPY ATSLRLSDLG
     YTNKSQSDLD ITFNHLETYV KGLKKAIHKP SEEFAKLGVK KDGKYIQLNT NVLQIENELY
     APIRPKRVVK GDESPSDALL RGGIEYIEVR SLDINPFTPI GVDETQIRFL DLFLIWCVLA
     DAPEMNAEEL ACCRANWNNV ILEGRKPGQV IGMGCGERKE PLAQVGKALF ADLQRVAKVL
     DSCSGTKYLE VCLKLEEMFD NPQLTFSGRL LEKIKAQGIG GYGLSLAEEY HQQLVNTAYE
     VLTDDAFEHE RISSIKRQAD LEKSDTISFD EYLKLHAGPN NDGVAS