ID A0A179UEE6_BLAGS Unreviewed; 217 AA.
AC A0A179UEE6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Glutathione S-transferase kappa {ECO:0000256|PIRNR:PIRNR006386};
DE EC=2.5.1.18 {ECO:0000256|PIRNR:PIRNR006386};
GN ORFNames=BDBG_02394 {ECO:0000313|EMBL:OAT06113.1};
OS Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT06113.1, ECO:0000313|Proteomes:UP000002038};
RN [1] {ECO:0000313|EMBL:OAT06113.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SLH14081 {ECO:0000313|EMBL:OAT06113.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center.;
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Klein B., Goldman B., Young S.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Heiman D.I.,
RA Hepburn T.A., Saif S., Shea T.D., Shenoy N., Sykes S., Galagan J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Blastomyces dermatitidis strain SLH14081.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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}.
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DR EMBL; GG657450; OAT06112.1; -; Genomic_DNA.
DR EMBL; GG657450; OAT06113.1; -; Genomic_DNA.
DR RefSeq; XP_002627723.1; XM_002627677.1.
DR AlphaFoldDB; A0A179UEE6; -.
DR VEuPathDB; FungiDB:BDBG_02394; -.
DR OrthoDB; 4159077at2759; -.
DR Proteomes; UP000002038; 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:UP000002038};
KW Transferase {ECO:0000256|PIRNR:PIRNR006386}.
FT DOMAIN 6..203
FT /note="DSBA-like thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF01323"
FT ACT_SITE 14
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006386-1"
SQ SEQUENCE 217 AA; 24146 MW; 3ED0FEE1CC865440 CRC64;
MAARKINLYL DVVSPFAYIA YFVTRHSPVF ANCHITYTPV FLGGILKACN NTSPIFVKNK
NKWTNTERLR WSKFLNVPMY PDMPKGFPIL TMSVQRALCA IPAEQLPACF DALYKELWVE
GNSQLNAPKT FLPILEAAVG KEMAANALEQ SNTQPIKDLL IANSDKAVET GAFGIPWFEC
TNSSGETECF WGVDRMAQVA AFLGLETTAD QGFRAMM
//