ID B6DTL8_BODSA Unreviewed; 263 AA.
AC B6DTL8;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
GN ORFNames=BSAL_28140 {ECO:0000313|EMBL:CUG90648.1};
OS Bodo saltans (Flagellated protozoan).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Eubodonida; Bodonidae; Bodo.
OX NCBI_TaxID=75058 {ECO:0000313|EMBL:ACI16063.1};
RN [1] {ECO:0000313|EMBL:ACI16063.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Lake Konstanz {ECO:0000313|EMBL:ACI16063.1};
RA Jackson A.P., Quail M.A., Berriman M.;
RT "Insights into the genome sequence of a free-living kinetoplastid: Bodo
RT saltans (Kinetoplastida: Euglenozoa).";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CUG90648.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Konstanz {ECO:0000313|EMBL:CUG90648.1};
RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000256|ARBA:ARBA00000280};
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
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DR EMBL; FJ168557; ACI16063.1; -; Genomic_DNA.
DR EMBL; CYKH01001852; CUG90648.1; -; Genomic_DNA.
DR VEuPathDB; TriTrypDB:BSAL_28140; -.
DR OMA; KPAPEWE; -.
DR OrthoDB; 47465at2759; -.
DR Proteomes; UP000051952; Unassembled WGS sequence.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR CDD; cd03015; PRX_Typ2cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10681:SF171; AT16346P-RELATED; 1.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000313|EMBL:ACI16063.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051952}.
FT DOMAIN 71..230
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 242..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 263 AA; 29043 MW; BDF4EC770DD4A37C CRC64;
MSQEHSTSDV TPPRKRDDIT HAQVADLTIS EGHDREDVFA SELEVRKELL IAADSVPTIK
VARKSPSVTH AQIGKPAPQF KTTALLANGT FGDVELSQYK GKWVVLFFYP LDFTFVCPTE
IIQFSDRAEE FRALNCEVIA ASVDSQFSHL AWTNTDRKKG GLGKMSIPIL ADLTKSVSTA
YGVLKEDEGI AFRGLFIIDP AQNLRQITIN DLPVGRNVDE TLRLLQAFQF VEEHGEVCPA
GWKPGSKSMK ADPKGSQEYF GAN
//
