ID   GSH1_PHOLL              Reviewed;         519 AA.
AC   Q7N7A4;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=plu1252;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(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; BX571863; CAE13546.1; -; Genomic_DNA.
DR   RefSeq; WP_011145576.1; NC_005126.1.
DR   AlphaFoldDB; Q7N7A4; -.
DR   SMR; Q7N7A4; -.
DR   STRING; 243265.plu1252; -.
DR   EnsemblBacteria; CAE13546; CAE13546; plu1252.
DR   GeneID; 24167403; -.
DR   KEGG; plu:plu1252; -.
DR   eggNOG; COG2918; Bacteria.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   OrthoDB; 967793at2; -.
DR   BioCyc; PLUM243265:PLU_RS06205-MON; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000002514; 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_0000192530"
SQ   SEQUENCE   519 AA;  58738 MW;  4F478A73A07BB2C0 CRC64;
     MIPDVSRALS WLEAHPTILK GIRRGVERET LRITSDGSLA ITEHPKTLGA ALTHKWITTD
     FAESLLEFIT PAGDDIKYTI SFLSDIHRHT ARVLDKEKMW PLSMPCFIDA EENITLAQYG
     ASNVGRYKTL YREGLKNRYG ALMQTISGVH YNFSLPIEFW RAWVGVEDAE SGKEQISNGY
     FRLIRNYYRF GWVIPYLFGA SPAICSSFLR GRETSFLFER TEDGTCYLPY ATSLRMSNLG
     YTNKSQSDLN ITFNNLHTYI DGLKKAIHKP SDEFAKLGTK QGDKHIQLNT NVLQIENELY
     APIRPKRVTR GNESPSDALL RGGVEYIEVR SLDINPFAAI GVNETQIRFL DLFLIWCVLA
     EAPEMGSDEL DCCRKNWNRV ILEGRKPGQM IGLGCGSVEE PLAKVGKKLF SDLKRVAAIL
     DSCSGTQYQK VCEELIATFD DSSLTLSARV LEKMKSQGIG GFGLELADEY HQQLISEKYE
     VISDEQFAIE RRASVERQDA LEREDTMSFD EYLKQQTGC