ID   GSH1_CANAX              Reviewed;         690 AA.
AC   Q9HF78;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Glutamate--cysteine ligase;
DE            EC=6.3.2.2;
DE   AltName: Full=Gamma-ECS;
DE            Short=GCS;
DE   AltName: Full=Gamma-glutamylcysteine synthetase;
GN   Name=GCS1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10231 / CBS 6431 / CIP 48.72 / DSM 1386 / NBRC 1594;
RA   Baek Y.-U., Kim Y.-R., Huh W.-K., Hwang C.-S., Kang C.-O.;
RT   "Molecular cloning and disruption of the gene encoding gamma
RT   glutamycysteine synthetase in Candida albicans.";
RL   Submitted (AUG-1999) 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   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC       L-cysteine and L-glutamate: step 1/2.
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 3 family.
CC       {ECO:0000305}.
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; AF176677; AAG43415.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HF78; -.
DR   SMR; Q9HF78; -.
DR   VEuPathDB; FungiDB:C1_07880C_A; -.
DR   VEuPathDB; FungiDB:CAWG_00632; -.
DR   UniPathway; UPA00142; UER00209.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046686; P:response to cadmium ion; IEA:EnsemblFungi.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:EnsemblFungi.
DR   InterPro; IPR004308; GCS.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   PANTHER; PTHR11164; PTHR11164; 1.
DR   Pfam; PF03074; GCS; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glutathione biosynthesis; Ligase; Nucleotide-binding.
FT   CHAIN           1..690
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_0000192569"
FT   REGION          574..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..618
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   690 AA;  79190 MW;  3926BE1E6BD5011D CRC64;
     MGLLSIGTPL SWDESKKYNN HVRTNGITQL INIFKQHGYR ENDVFLWGDE VEYMLVDFDE
     TKKTARLSID KDYIINDLND PDKLLPIAEK QDVSYHPEYG RFMVEATPAK PYNGNLLSDY
     LYIEKNMIIR RQLCEDNLPS HIKLLTLTTF PRMGCNIFTS PPSKPDGIAS QSLFLPDEII
     NRHARFPTLT ANIRKRKGHK VAINLPIYPD KSTKLLDDTI PQNRELFDSD KEPWIGASKP
     GFIYMDSMGF GMGSSCLQIT MQTKNISQAR YLYDSLAPIA PIMLSLSAAA PIFKGFLVDQ
     DVRWNVVSGA VDDRTFIEKG QEPYSGYHLF GGLDIDAQDK LRINNHQINQ QGDLLDLYTK
     DGKPIQRVPQ SRYDSIDNYL NDNYYDTKYF QDEYNDLNAP INEQVYQRLI DEGKLDKYMA
     NHFAHLFIRD PLVIFSERIN QDNNLENDHF ENIQSTNWQT LRFKPPALYT KDTDLTTKPG
     WRVEFRPMEI QLTDFENAAY SSFITLLSKA ILKFQPNFYI PLSKVEINMK LAHKVDSTLK
     DKFWFRSFEL WNIDPQEFDD YGFEWFDQFI NGNQQQNGHV NNNNNNDKKT KNDPIIVNGS
     TTTTNGTNSG SGITETNGTM LPKGCEGKTV EEINDVDDNG IDQRYTICQL INGSGEFPGF
     IKLVIKLIAT DLVPQALNNS TISKEQLIEN