ID A0A1L9UQS2_ASPBC Unreviewed; 612 AA. AC A0A1L9UQS2; DT 15-MAR-2017, integrated into UniProtKB/TrEMBL. DT 15-MAR-2017, sequence version 1. DT 25-MAY-2022, entry version 18. DE RecName: Full=Glutamate--cysteine ligase {ECO:0000256|ARBA:ARBA00012220, ECO:0000256|RuleBase:RU367135}; DE EC=6.3.2.2 {ECO:0000256|ARBA:ARBA00012220, ECO:0000256|RuleBase:RU367135}; DE AltName: Full=Gamma-ECS {ECO:0000256|ARBA:ARBA00032122, ECO:0000256|RuleBase:RU367135}; DE AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000256|ARBA:ARBA00030585, ECO:0000256|RuleBase:RU367135}; GN ORFNames=ASPBRDRAFT_194901 {ECO:0000313|EMBL:OJJ74011.1}; OS Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=767769 {ECO:0000313|EMBL:OJJ74011.1, ECO:0000313|Proteomes:UP000184499}; RN [1] {ECO:0000313|Proteomes:UP000184499} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 101740 {ECO:0000313|Proteomes:UP000184499}; RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0; RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S., RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E., RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D., RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A., RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S., RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B., RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z., RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A., RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A., RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M., RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P., RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F., RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J., RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M., RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V., RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E., RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C., RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E., RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C., RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C., RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.; RT "Comparative genomics reveals high biological diversity and specific RT adaptations in the industrially and medically important fungal genus RT Aspergillus."; RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017). 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:0000256|RuleBase:RU367135}; CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from CC L-cysteine and L-glutamate: step 1/2. {ECO:0000256|ARBA:ARBA00005006, CC ECO:0000256|RuleBase:RU367135}. CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 3 family. CC {ECO:0000256|ARBA:ARBA00008100, ECO:0000256|RuleBase:RU367135}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KV878682; OJJ74011.1; -; Genomic_DNA. DR STRING; 767769.A0A1L9UQS2; -. DR EnsemblFungi; OJJ74011; OJJ74011; ASPBRDRAFT_194901. DR VEuPathDB; FungiDB:ASPBRDRAFT_194901; -. DR OrthoDB; 575052at2759; -. DR UniPathway; UPA00142; UER00209. DR Proteomes; UP000184499; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniRule. 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 {ECO:0000256|RuleBase:RU367135}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Glutathione biosynthesis {ECO:0000256|RuleBase:RU367135}; KW Ligase {ECO:0000256|RuleBase:RU367135}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU367135}; KW Reference proteome {ECO:0000313|Proteomes:UP000184499}. FT COILED 454..474 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 612 AA; 69870 MW; 9329BD418C2FFD3E CRC64; MGPPVSGTPL SWQELQKVAP IARQGAVEQL LSLWKRQRGR SDPEPLWGDE IEYTLVSLNP STSRATLLLN QEDILRKEEL QCASAQEVEP WNEVKLQAEW ARHMVEATPG EPYGGDILDL LRVEGNMKRR RKLIGQYLSP DQHPVPLCVF PGLGERGQFT LPESPHEASL EQICCPIPRY IMMTQNLLAR RQRRVESYIP VFRDEQTKAP FHDNSVSFEY PAVHPPGNGK EGHVHLDGIG LGVGNCCIQV TFQAPNEIEA RWLHDQMIAL GPVMLALTAA TPIYKGYLVD TEVRWDRTSE CFDDRTPEEL ATTPPRYSWN RTYISQEKPA NLDSKYPLTP MNESVKQRLL DGGMDEPLAM HYATILSRDP IVLNRTDLED FDLNSTGIFD VYYSTVWQHV RLKIPLSDDG PGWRVEFRPM EVQLTDFDNA AFAIFMYLLS RAITELHLNF YVPIDQLGDS MERAQKRNAA LEERFWFRRT GWSSAEQCER PPRQRKGCVN CCSKSNAHAS PSCALLTADE IINGEDPKVP SSFPGLVNIV RAWLQYNNTP VPEQKKIMPY LDVISKRASG ELPTPAQWMR SFVTGHEEYQ RDSYVSEKIR YDLIQEIVRM VD //