ID A1CN39_ASPCL Unreviewed; 215 AA. AC A1CN39; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 83. DE RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452}; DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452}; GN ORFNames=ACLA_099200 {ECO:0000313|EMBL:EAW08976.1}; OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / OS NRRL 1 / QM 1276 / 107). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW08976.1, ECO:0000313|Proteomes:UP000006701}; RN [1] {ECO:0000313|EMBL:EAW08976.1, ECO:0000313|Proteomes:UP000006701} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 RC {ECO:0000313|Proteomes:UP000006701}; RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046; RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M., RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.; RT "Genomic islands in the pathogenic filamentous fungus Aspergillus RT fumigatus."; RL PLoS Genet. 4:E1000046-E1000046(2008). CC -!- CATALYTIC ACTIVITY: CC Reaction=glutathione + RX = a halide anion + an S-substituted CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, CC ChEBI:CHEBI:90779; EC=2.5.1.18; CC Evidence={ECO:0000256|ARBA:ARBA00000710}; CC -!- SIMILARITY: Belongs to the GST superfamily. CC {ECO:0000256|RuleBase:RU003494}. 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; DS027058; EAW08976.1; -; Genomic_DNA. DR RefSeq; XP_001270402.1; XM_001270401.1. DR AlphaFoldDB; A1CN39; -. DR STRING; 344612.A1CN39; -. DR EnsemblFungi; EAW08976; EAW08976; ACLA_099200. DR GeneID; 4702177; -. DR KEGG; act:ACLA_099200; -. DR VEuPathDB; FungiDB:ACLA_099200; -. DR eggNOG; KOG0867; Eukaryota. DR HOGENOM; CLU_011226_5_1_1; -. DR OMA; NVKKVRW; -. DR OrthoDB; 639740at2759; -. DR Proteomes; UP000006701; Unassembled WGS sequence. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf. DR InterPro; IPR040079; Glutathione_S-Trfase. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR004046; GST_C. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR43900:SF98; GLUTATHIONE S-TRANSFERASE 2; 1. DR PANTHER; PTHR43900; GLUTATHIONE S-TRANSFERASE RHO; 1. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1. DR SFLD; SFLDG01154; Main.5:_Phi-like; 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. PE 3: Inferred from homology; KW Reference proteome {ECO:0000313|Proteomes:UP000006701}. FT DOMAIN 1..85 FT /note="GST N-terminal" FT /evidence="ECO:0000259|PROSITE:PS50404" FT DOMAIN 94..215 FT /note="GST C-terminal" FT /evidence="ECO:0000259|PROSITE:PS50405" SQ SEQUENCE 215 AA; 24565 MW; C1EE9234A614B257 CRC64; MVLKINGHPS STCTMRVRTV LAEKGLDYEL HTVDLMKGEQ KTQTYLNELQ PFGKIPVLQD TENGVQIYES RAIAQYIINK YRGQGTELAP PESDLKAWAL YQQALSIEQS YFDPVVYGIA YEKVFKSLKG HGETDAARVQ ALLSQLDLAL QGYERVLSKQ KYLAGDQLTF ADLAHLPYGV FVEQFGFAEL IPKYPHFQKW WEELKARESW KKVNA //