ID A0A0L0HU20_SPIPD Unreviewed; 208 AA.
AC A0A0L0HU20;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Glutathione S-transferase kappa {ECO:0000256|PIRNR:PIRNR006386};
DE EC=2.5.1.18 {ECO:0000256|PIRNR:PIRNR006386};
GN ORFNames=SPPG_00103 {ECO:0000313|EMBL:KND04374.1};
OS Spizellomyces punctatus (strain DAOM BR117).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Spizellomycetales;
OC Spizellomycetaceae; Spizellomyces.
OX NCBI_TaxID=645134 {ECO:0000313|EMBL:KND04374.1, ECO:0000313|Proteomes:UP000053201};
RN [1] {ECO:0000313|EMBL:KND04374.1, ECO:0000313|Proteomes:UP000053201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM BR117 {ECO:0000313|EMBL:KND04374.1,
RC ECO:0000313|Proteomes:UP000053201};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T.,
RA White J., Yandava C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Lander E., Nusbaum C.;
RT "The Genome Sequence of Spizellomyces punctatus strain DAOM BR117.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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|PIRNR:PIRNR006386};
CC -!- SIMILARITY: Belongs to the GST superfamily. Kappa family.
CC {ECO:0000256|PIRNR:PIRNR006386}.
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; KQ257450; KND04374.1; -; Genomic_DNA.
DR RefSeq; XP_016612413.1; XM_016748440.1.
DR AlphaFoldDB; A0A0L0HU20; -.
DR STRING; 645134.A0A0L0HU20; -.
DR GeneID; 27683855; -.
DR VEuPathDB; FungiDB:SPPG_00103; -.
DR eggNOG; ENOG502R0HS; Eukaryota.
DR InParanoid; A0A0L0HU20; -.
DR OMA; YPCATRE; -.
DR OrthoDB; 4159077at2759; -.
DR Proteomes; UP000053201; Unassembled WGS sequence.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR InterPro; IPR014440; HCCAis_GSTk.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR42943; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR PANTHER; PTHR42943:SF2; GLUTATHIONE S-TRANSFERASE KAPPA 1; 1.
DR Pfam; PF01323; DSBA; 1.
DR PIRSF; PIRSF006386; HCCAis_GSTk; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053201};
KW Transferase {ECO:0000256|PIRNR:PIRNR006386}.
FT DOMAIN 7..196
FT /note="DSBA-like thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF01323"
FT ACT_SITE 15
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006386-1"
SQ SEQUENCE 208 AA; 23517 MW; 2A383CFCDDCE2EDE CRC64;
MPVRPSIKFY YDVVSPYSYI AFHLLRRYRP TWNFDLVLVP MFLGFTLKNV GTPPPAFNPV
KVEYMRKDIG RIKTIHNIEM NVFPNPFPAN TLKAMRLLHA IKLQGSAEVL EDATVKLFAS
YWTKGEDIAS PQVLASCVEG EEYLKAMETQ QVKDSLVALS KEVVEKGVFG APTMLVDRGD
GKAEVFFGSD RLDHVAWFLG KEVPKAKM
//
