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Database: UniProt/TrEMBL
Entry: B3RQ56_TRIAD
LinkDB: B3RQ56_TRIAD
Original site: B3RQ56_TRIAD 
ID   B3RQ56_TRIAD            Unreviewed;       239 AA.
AC   B3RQ56;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=Glutathione transferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TRIADDRAFT_21044 {ECO:0000313|EMBL:EDV28295.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV28295.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV28295.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV28295.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
CC   -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC       {ECO:0000256|ARBA:ARBA00011067}.
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DR   EMBL; DS985242; EDV28295.1; -; Genomic_DNA.
DR   RefSeq; XP_002110129.1; XM_002110093.1.
DR   AlphaFoldDB; B3RQ56; -.
DR   STRING; 10228.B3RQ56; -.
DR   EnsemblMetazoa; TriadT21044; TriadP21044; TriadG21044.
DR   GeneID; 6750812; -.
DR   KEGG; tad:TRIADDRAFT_21044; -.
DR   CTD; 6750812; -.
DR   eggNOG; KOG0406; Eukaryota.
DR   HOGENOM; CLU_011226_9_2_1; -.
DR   InParanoid; B3RQ56; -.
DR   OMA; WYTDYSP; -.
DR   OrthoDB; 103277at2759; -.
DR   PhylomeDB; B3RQ56; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IBA:GO_Central.
DR   GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR   GO; GO:0050610; F:methylarsonate reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR   CDD; cd00570; GST_N_family; 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; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR005442; GST_omega.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43968; -; 1.
DR   PANTHER; PTHR43968:SF6; GLUTATHIONE-DEPENDENT DEHYDROASCORBATE REDUCTASE; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01625; GSTRNSFRASEO.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT   DOMAIN          18..96
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          75..224
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   239 AA;  27747 MW;  2CA5326F9F8DD276 CRC64;
     MAKVIQLQKG DSKPSSTKDL KLYGMRFDPY SMALRLIMRR KGLDFDFYSI KMSDRPDFLQ
     QLNPNGQIPV LEHGDTVVYE TIIIYEYLED TFTDKPLRSS DPATRAMDRI FLHEIYTNLP
     PVIRAMMEGI EAKRLLDQLL RVENRLQKQG SPYFGGNEPN YIDFMVWSWL ELIPALKRAF
     TLTFELPRGS FSNTWAWIGR MDKEPVINAE RKASRVNAEI RSRFFKSVAD GSPDYMVGL
//
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