ID   GSH1_SCHPO              Reviewed;         669 AA.
AC   Q09768;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   16-JUN-2009, entry version 63.
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=gcs1; ORFNames=SPAC22F3.10c;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D18;
RX   MEDLINE=96109929; PubMed=8619315; DOI=10.1002/yea.320111207;
RA   Coblenz A., Wolf K.;
RT   "Gcs1, a gene encoding gamma-glutamylcysteine synthetase in the
RT   fission yeast Schizosaccharomyces pombe.";
RL   Yeast 11:1171-1177(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95332248; PubMed=7608113;
RA   Mutoh N.;
RT   "Molecular cloning and nucleotide sequencing of the gamma-
RT   glutamylcysteine synthetase gene of the fission yeast
RT   Schizosaccharomyces pombe.";
RL   J. Biochem. 117:283-288(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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   -!- SUBUNIT: Heterodimer of a catalytic heavy chain and a regulatory
CC       light chain (By similarity).
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 3
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X85017; CAA59379.1; -; Genomic_DNA.
DR   EMBL; D55676; BAA09527.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAA91075.1; -; Genomic_DNA.
DR   PIR; T38181; T38181.
DR   RefSeq; NP_593031.1; -.
DR   GeneID; 2541881; -.
DR   KEGG; spo:SPAC22F3.10c; -.
DR   NMPDR; fig|4896.1.peg.3001; -.
DR   GeneDB_Spombe; SPAC22F3.10c; -.
DR   OMA; Q09768; FNTVEDN.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-000751-MON; -.
DR   BRENDA; 6.3.2.2; 653.
DR   ArrayExpress; Q09768; -.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe.
DR   GO; GO:0005634; C:nucleus; IDA:GeneDB_SPombe.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IMP:GeneDB_SPombe.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IMP:GeneDB_SPombe.
DR   GO; GO:0046686; P:response to cadmium ion; IMP:GeneDB_SPombe.
DR   InterPro; IPR004308; GCS.
DR   PANTHER; PTHR11164; GCS; 1.
DR   Pfam; PF03074; GCS; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Glutathione biosynthesis; Ligase;
KW   Nucleotide-binding.
FT   CHAIN         1    669       Glutamate--cysteine ligase.
FT                                /FTId=PRO_0000192571.
FT   CONFLICT     28     28       M -> I (in Ref. 1).
FT   CONFLICT     79    123       Missing (in Ref. 1; CAA59379).
FT   CONFLICT    105    105       K -> N (in Ref. 2; BAA09527).
FT   CONFLICT    399    399       E -> A (in Ref. 2; BAA09527).
SQ   SEQUENCE   669 AA;  76523 MW;  CE676112B1FB768C CRC64;
     MGLLVLGTPL DWPESKKYCD YVRENGIMQF LHMYDTYISK KQDVLLWGDE IECIVVSMDD
     KSKKARVSLR QEDILNALGK YEETFRHVDF GPVYAALRNE TCPKKIDAIL SEVAKNPADY
     VERIGGNSNK DTIEITSSTK PHAQNAVPTF HPEYGRYMLE STPGAPYGST LKDFTFVEYN
     MRLRRKIIEN HLLPNELPLT ITNFFRLGTP GFTDPEVEAN GAISRSFFLP DDVINTHVRF
     PTLTANIRQR RGRKVAMNVP IFFDKNTIKP FHDPTVPWDR NLFPEDANAR DGAALDNHIY
     MDSMGFGMGC CCLQITFQAK SCDEARLLYD QLTPITPLML ALSAGTPAFR GYLADQDCRW
     NVIAGAVDDR TEEEMKTVPK SRYDSVDLYI SNDKRNLPEY NDVPVVINQD CYDKLIKDCI
     DERLAKHMAH IFSRDPLVIF SDSILQDNSV SNAHFENLNS TNWQSMRFKP PPPGSDIGWR
     VEFRSMEIQI TDFENAAYSI FVVMLSRAIL SFNLNLYMPI SLVDENMKAA HARDAIHRKK
     FWFRCNPFPD ASTDDESGQF RQLTIDELFN GEHRENGFPG LITIVRSYLY SCNPDAKTIC
     LIERYIRLIS QRANGQCLTA ASWIRNFITT HPSYKQDSVV NDEINYDLIR RIAKIVDGDY
     DDTLLGKCS
//