ID   GSH1_CAEEL              Reviewed;         654 AA.
AC   Q20117;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   11-APR-2003, sequence version 2.
DT   16-JUN-2009, entry version 53.
DE   RecName: Full=Glutamate--cysteine ligase;
DE            EC=6.3.2.2;
DE   AltName: Full=Gamma-glutamylcysteine synthetase;
DE   AltName: Full=Gamma-ECS;
DE            Short=GCS;
GN   Name=gcs-1; ORFNames=F37B12.2;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + L-cysteine = ADP +
CC       phosphate + gamma-L-glutamyl-L-cysteine.
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
CC       from L-cysteine and L-glutamate: step 1/2.
CC   -!- INTERACTION:
CC       Q966L2:-; NbExp=2; IntAct=EBI-311822, EBI-311817;
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 3
CC       family.
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DR   EMBL; Z54218; CAA90955.2; -; Genomic_DNA.
DR   PIR; T21908; T21908.
DR   RefSeq; NP_495927.2; -.
DR   UniGene; Cel.17240; -.
DR   IntAct; Q20117; 1.
DR   Ensembl; F37B12.2; Caenorhabditis elegans.
DR   GeneID; 174438; -.
DR   KEGG; cel:F37B12.2; -.
DR   WormBase; WBGene00001527; gcs-1.
DR   WormPep; F37B12.2; CE32886.
DR   OMA; Q20117; FNTVEDN.
DR   BRENDA; 6.3.2.2; 672.
DR   NextBio; 884042; -.
DR   ArrayExpress; Q20117; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR004308; GCS.
DR   PANTHER; PTHR11164; GCS; 1.
DR   Pfam; PF03074; GCS; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Glutathione biosynthesis; Ligase;
KW   Nucleotide-binding.
FT   CHAIN         1    654       Glutamate--cysteine ligase.
FT                                /FTId=PRO_0000192566.
SQ   SEQUENCE   654 AA;  74369 MW;  37EA2F5DFC2BEAB5 CRC64;
     MGLLTKGSPL TWAETVPHID YIKKHGIAQF INLYHRLKSR HGDQLKWGDE IEYTIVKFDD
     ANKKVRVSCK AEELLNKLQA EEQVNAMLGT ANRFLWRPEF GSYMIEGTPG MPYGGLIACF
     NIVEANMKLR RQVVKKLLKK DETCLSISFP SLGVPGFTFP EVAADRKNDD AANSVFWPEQ
     AVFLGHPRFK NLTKNIKGRR GSKVAINVPI FKDTNTPSPF VEDLSALGGP DDTRDAKPDH
     IYMDHMGFGM GCCCLQVTFQ AVNVDEARWL YDQLTPITPI LLALSAATPI FRGKLSNVDS
     RWDIISASVD DRTPEERGLE PLKNSKWVID KSRYDSTDCY IYPCSVGYND IPLQYDETIY
     KQLIDGNIDE PLAKHIAHMF IRDPHQVFRE RIEQDDEKSS EHFETIQSSN WMNMRFKPPP
     PDAPEIGWRV EFRPTEVQLT DFENAAYCCF VVLLTRMMIS FRLTYLMPIS MVTENMKRAQ
     QKDAVLNQKF LFRKGLAECK SAPENLKGSE KCGPPSQDIE EMSIDEIING KKNGFPGLIS
     LIRQFLDSAD VDVDTRCTIS QYLNFISKRA TGEINTLAHW TRGFVQSHPA YKHDSDVNDN
     IVYDLLKKMD AISNGEDHCE KLLGCYRSKT DHAISAAVRK AEEHMIVSSQ KRAH
//