GSH1_DICDI
ID GSH1_DICDI Reviewed; 626 AA.
AC Q54PC2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Glutamate--cysteine ligase;
DE EC=6.3.2.2 {ECO:0000305|PubMed:15993406};
DE AltName: Full=Gamma-ECS;
DE Short=GCS {ECO:0000303|PubMed:15993406};
DE AltName: Full=Gamma-glutamylcysteine synthetase;
GN Name=gcsA; Synonyms=gshA; ORFNames=DDB_G0284651;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15993406; DOI=10.1016/j.ydbio.2005.05.034;
RA Kim B.-J., Choi C.-H., Lee C.-H., Jeong S.-Y., Kim J.-S., Kim B.-Y.,
RA Yim H.-S., Kang S.-O.;
RT "Glutathione is required for growth and prespore cell differentiation in
RT Dictyostelium.";
RL Dev. Biol. 284:387-398(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: An essential enzyme in glutathione (L-gamma-glutamyl-L-
CC cysteinylglycine, GSH) biosynthesis, GSH is essential for growth and
CC differentiation to prespore stage (PubMed:15993406). Catalyzes the
CC condensation of glutamate to cysteine (PubMed:15993406).
CC {ECO:0000269|PubMed:15993406, ECO:0000303|PubMed:15993406}.
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:15993406};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13286;
CC Evidence={ECO:0000305|PubMed:15993406};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 1/2.
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, expression
CC peaking at the aggregation stage. Expression is localized in the
CC prespore region and tip region of the tipped aggregate. At slug stage,
CC expression is predominantly in the posterior prespore region. In the
CC fruiting body expression is detected in basal disk and spore region
CC containing upper cup and lower cup. {ECO:0000269|PubMed:15993406}.
CC -!- DISRUPTION PHENOTYPE: Cells show defects in prespore differentiation.
CC {ECO:0000269|PubMed:15993406}.
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 3 family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000070; EAL65095.1; -; Genomic_DNA.
DR RefSeq; XP_638453.1; XM_633361.1.
DR AlphaFoldDB; Q54PC2; -.
DR SMR; Q54PC2; -.
DR STRING; 44689.DDB0231403; -.
DR PaxDb; Q54PC2; -.
DR PRIDE; Q54PC2; -.
DR EnsemblProtists; EAL65095; EAL65095; DDB_G0284651.
DR GeneID; 8624704; -.
DR KEGG; ddi:DDB_G0284651; -.
DR dictyBase; DDB_G0284651; gcsA.
DR eggNOG; KOG3754; Eukaryota.
DR HOGENOM; CLU_010467_0_0_1; -.
DR InParanoid; Q54PC2; -.
DR OMA; YISQDPR; -.
DR PhylomeDB; Q54PC2; -.
DR UniPathway; UPA00142; UER00209.
DR PRO; PR:Q54PC2; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IMP:UniProtKB.
DR GO; GO:0006750; P:glutathione biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
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 1: Evidence at protein level;
KW ATP-binding; Developmental protein; Differentiation;
KW Glutathione biosynthesis; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..626
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_0000327705"
SQ SEQUENCE 626 AA; 71956 MW; F3FBC32BE56A8C88 CRC64;
MGFIAEGNTL AWEDSVKYLE YIREHGVIQL LNIIKNNKDK VTEDFKWGDE VEYILINNDN
YKLKLRANEI LDLLMLEEKR NPTTVEHLWR PEYGRFMIEG TPGSPYIGLG KQLLSIQSNL
KSRRENVEKY LKPNESILTI TSYPRMGCKN FTDPQGEVKG PIAESKFLPD TVINPHFRFS
TLTANIRKRR GGTVSINIPM YRDKNTPEYL DQICTYEKVP PILDDSDNSQ TNISSPSNQP
FNIYMDAMGF GMGCCCLQTT FQLPNIDDAR TVYDQLAPIS PLMLSLTAAS SIFKGYLSDI
DARWTIISQS VDDRNKEELG KAPLNNNKFV INKSRYDSID SYIGSKSKSF RSEYNDLDLV
YDKDVYQKLI ENGVDSLLSK HFAHLFIRDP LVIYSDKIEI DDEKNTDHFE NIQSTNWQTV
RFKPPPPSSS IGWRVELRPM EVQLTDFQNS AFVVFSAILV KAIQDLKLNF YIPITKVDEN
LKTAHKRASV INDKFYFRKN IYNNTPNGSI ENEYELMTIN EIFNGKGGDN KGLIGVIRDY
ISTLDFDNET TELVNKYIKF ISKRASGEIK SISTWTREFV QNHPAYNHDS IVNDEIQADY
LQRCLDISNG TIYDSSIQGD KDDYYC
