GSH1_SCHPO
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 03-AUG-2022, entry version 144.
DE RecName: Full=Glutamate--cysteine ligase;
DE EC=6.3.2.2 {ECO:0000305|PubMed:8619315};
DE AltName: Full=Gamma-ECS;
DE Short=GCS;
DE AltName: Full=Gamma-glutamylcysteine synthetase;
GN Name=gcs1; ORFNames=SPAC22F3.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=D18;
RX PubMed=8619315; DOI=10.1002/yea.320111207;
RA Coblenz A., Wolf K.;
RT "Gcs1, a gene encoding gamma-glutamylcysteine synthetase in the fission
RT yeast Schizosaccharomyces pombe.";
RL Yeast 11:1171-1177(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7608113; DOI=10.1093/jb/117.2.283;
RA Mutoh N.;
RT "Molecular cloning and nucleotide sequencing of the gamma-glutamylcysteine
RT synthetase gene of the fission yeast Schizosaccharomyces pombe.";
RL J. Biochem. 117:283-288(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX 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., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Catalyzes the ATP-dependent ligation of L-glutamate and L-
CC cysteine and participates in the first and rate-limiting step in
CC glutathione biosynthesis. {ECO:0000305|PubMed:8619315}.
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:0000305|PubMed:8619315};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 1/2. {ECO:0000305|PubMed:8619315}.
CC -!- SUBUNIT: Heterodimer of a catalytic heavy chain and a regulatory light
CC chain. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 3 family.
CC {ECO:0000305}.
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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; NM_001018430.2.
DR AlphaFoldDB; Q09768; -.
DR SMR; Q09768; -.
DR BioGRID; 278371; 5.
DR STRING; 4896.SPAC22F3.10c.1; -.
DR iPTMnet; Q09768; -.
DR MaxQB; Q09768; -.
DR PaxDb; Q09768; -.
DR PRIDE; Q09768; -.
DR EnsemblFungi; SPAC22F3.10c.1; SPAC22F3.10c.1:pep; SPAC22F3.10c.
DR GeneID; 2541881; -.
DR KEGG; spo:SPAC22F3.10c; -.
DR PomBase; SPAC22F3.10c; gcs1.
DR VEuPathDB; FungiDB:SPAC22F3.10c; -.
DR eggNOG; KOG3754; Eukaryota.
DR HOGENOM; CLU_010467_0_0_1; -.
DR InParanoid; Q09768; -.
DR OMA; YISQDPR; -.
DR PhylomeDB; Q09768; -.
DR BRENDA; 6.3.2.2; 5613.
DR Reactome; R-SPO-174403; Glutathione synthesis and recycling.
DR UniPathway; UPA00142; UER00209.
DR PRO; PR:Q09768; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0017109; C:glutamate-cysteine ligase complex; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IMP:PomBase.
DR GO; GO:0098849; P:cellular detoxification of cadmium ion; IMP:PomBase.
DR GO; GO:0071276; P:cellular response to cadmium ion; IMP:PomBase.
DR GO; GO:0006534; P:cysteine metabolic process; IC:PomBase.
DR GO; GO:0006750; P:glutathione biosynthetic process; IMP:PomBase.
DR GO; GO:0046938; P:phytochelatin biosynthetic process; IMP:PomBase.
DR InterPro; IPR004308; GCS.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR11164; PTHR11164; 1.
DR Pfam; PF03074; GCS; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Glutathione biosynthesis; Ligase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..669
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_0000192571"
FT CONFLICT 28
FT /note="M -> I (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 79..123
FT /note="Missing (in Ref. 1; CAA59379)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="K -> N (in Ref. 2; BAA09527)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="E -> A (in Ref. 2; BAA09527)"
FT /evidence="ECO:0000305"
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
