ID   GSH1_NEUCR              Reviewed;         728 AA.
AC   Q8X0X0; Q7S804;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 113.
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=gcs-1; ORFNames=123A4.220, NCU01157;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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}.
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DR   EMBL; AL670009; CAD21373.1; -; Genomic_DNA.
DR   EMBL; CM002240; EAA32287.1; -; Genomic_DNA.
DR   RefSeq; XP_961523.1; XM_956430.2.
DR   AlphaFoldDB; Q8X0X0; -.
DR   SMR; Q8X0X0; -.
DR   STRING; 5141.EFNCRP00000004432; -.
DR   EnsemblFungi; EAA32287; EAA32287; NCU01157.
DR   GeneID; 3877703; -.
DR   KEGG; ncr:NCU01157; -.
DR   VEuPathDB; FungiDB:NCU01157; -.
DR   HOGENOM; CLU_010467_0_0_1; -.
DR   InParanoid; Q8X0X0; -.
DR   OMA; YISQDPR; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR   GO; GO:0017109; C:glutamate-cysteine ligase complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IBA:GO_Central.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IBA:GO_Central.
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;
KW   Reference proteome.
FT   CHAIN           1..728
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_0000192570"
FT   REGION          517..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..545
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   728 AA;  81879 MW;  CF0C5907DBDD5AC0 CRC64;
     MGLLALGTAL DWPDAKQQAH LVRAWGIKQL LEIWNKAKGK ERDAMLWGDE IEYLVVNYSK
     DEPKVLLSLR QADILKALAD SKTLKVTGDC APGTEANADA GNVTLPVFHP EFGRFMLEAT
     PGKPWGIDFK DLLTVEADMK LRRCIAKDHM LSNEHPITLT TFPRIGSPGV FTEPSYPVSG
     PKLRSQFVPD EIANPHIRFP TLAANIRSRR GRKVQVNVPV FRDENTPWPW KDPTVNYDLH
     NWPEDDDVRN GAAPDNFIHM DAMAFGMGSC CLQITFQAKN ITEGRKMYDQ LSPLGPILLA
     LTAATPVYKG FIADTDVRWN QISRAVDDRT PEELGEKPLK NDRWRIPKSR YASNSTYIST
     DSRLRPEYMD PNLVIDPEIK QQLLDGGMDD RLATHFAHLF IRDPIVIFNE DLQELDLTKT
     DHFENIQSTN WQHMRFKPPP ADNSIGWRVE FRPMEIQITD FENAAFSVFI VLITRAILSF
     DLNFYIPIVK VDENMETAHA RNANLEKKFW FRKNPFPVRT TRRGGSASRS ASGTSTPNSG
     SSRPATPPLG PVEDEYRLMS VNEVINGTAY AKATSKEVTE DAEEGEEFPG LIPLVESYLD
     SVNMDVATRC GLARYLDLIR KRASGELWTA AKWIREFIAK HPGYKKDSVV SEEITKDLVG
     AVIEIGEREK RGLGIDDLIG QVPDLEKLFG GFLKGKSPCG GGQAALEQKL KDDDAKVNGV
     KRKFNEEQ