ID D8SVE8_SELML Unreviewed; 228 AA. AC D8SVE8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAR-2024, entry version 62. DE RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452}; DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452}; GN ORFNames=SELMODRAFT_125797 {ECO:0000313|EMBL:EFJ11601.1}; OS Selaginella moellendorffii (Spikemoss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella. OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514}; RN [1] {ECO:0000313|EMBL:EFJ11601.1, ECO:0000313|Proteomes:UP000001514} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551031; DOI=10.1126/science.1203810; RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M., RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W., RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D., RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I., RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K., RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M., RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G., RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y., RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K., RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R., RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B., RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y., RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N., RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N., RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S., RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q., RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J., RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.; RT "The Selaginella genome identifies genetic changes associated with the RT evolution of vascular plants."; RL Science 332:960-963(2011). 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 --------------------------------------------------------------------------- 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; GL377645; EFJ11601.1; -; Genomic_DNA. DR RefSeq; XP_002987286.1; XM_002987240.1. DR AlphaFoldDB; D8SVE8; -. DR STRING; 88036.D8SVE8; -. DR EnsemblPlants; EFJ11601; EFJ11601; SELMODRAFT_125797. DR Gramene; EFJ11601; EFJ11601; SELMODRAFT_125797. DR KEGG; smo:SELMODRAFT_125797; -. DR eggNOG; KOG0406; Eukaryota. DR HOGENOM; CLU_011226_18_0_1; -. DR InParanoid; D8SVE8; -. DR OMA; QCGRMHK; -. DR Proteomes; UP000001514; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central. DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central. DR GO; GO:0042221; P:response to chemical; IEA:UniProt. DR CDD; cd03185; GST_C_Tau; 1. 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; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR045074; GST_C_Tau. DR InterPro; IPR045073; Omega/Tau-like. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR11260:SF781; GLUTATHIONE S-TRANSFERASE U22; 1. DR PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1. DR Pfam; PF13410; GST_C_2; 1. DR Pfam; PF02798; GST_N; 1. DR SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 1. DR SFLD; SFLDG00358; Main_(cytGST); 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 4: Predicted; KW Reference proteome {ECO:0000313|Proteomes:UP000001514}. FT DOMAIN 2..83 FT /note="GST N-terminal" FT /evidence="ECO:0000259|PROSITE:PS50404" FT DOMAIN 90..217 FT /note="GST C-terminal" FT /evidence="ECO:0000259|PROSITE:PS50405" SQ SEQUENCE 228 AA; 25855 MW; 6A1DAC4911069A91 CRC64; MAEVTLLSLP ASPFAMSVKM ALIEKGVEFE TVEENYRASG KSELLVRVNP VTKQVPVLLH RAKPIWESLV ILEYVEETWK TQGTHLLPGD GYQRALARFW TNFVITKTGL LIMKRVGDEQ LKARDQVLEM IRLMDSEWSK PEYGKPFVFG DKLSLADLAL APIASWKVTF ETLGKFEFPD ARTCPRMALW LDAIENHPTV QSAILAPDLN LENANVIQKL IKDNKIKF //