ID A0A0K2YEK6_9NOCA Unreviewed; 177 AA.
AC A0A0K2YEK6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000256|ARBA:ARBA00032824};
GN Name=bcp {ECO:0000313|EMBL:CRK49190.1};
GN ORFNames=RHCRD62_10045 {ECO:0000313|EMBL:CRK49190.1};
OS Rhodococcus sp. RD6.2.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=260936 {ECO:0000313|EMBL:CRK49190.1, ECO:0000313|Proteomes:UP000044872};
RN [1] {ECO:0000313|EMBL:CRK49190.1, ECO:0000313|Proteomes:UP000044872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RD6.2 {ECO:0000313|EMBL:CRK49190.1,
RC ECO:0000313|Proteomes:UP000044872};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides and as sensor of hydrogen peroxide-mediated
CC signaling events. {ECO:0000256|ARBA:ARBA00003330}.
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC {ECO:0000256|ARBA:ARBA00038489}.
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DR EMBL; CVQP01000001; CRK49190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K2YEK6; -.
DR STRING; 260936.RHCRD62_10045; -.
DR Proteomes; UP000044872; Unassembled WGS sequence.
DR GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; IEA:RHEA.
DR CDD; cd03017; PRX_BCP; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR42801:SF24; PEROXIREDOXIN BCP; 1.
DR PANTHER; PTHR42801; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE; 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 Oxidoreductase {ECO:0000313|EMBL:CRK49190.1};
KW Peroxidase {ECO:0000313|EMBL:CRK49190.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000044872}.
FT DOMAIN 27..177
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 177 AA; 19404 MW; 4B60D67F6F213012 CRC64;
MVGLSCHDRT RRRPTSSLTI VTDNIRLAPG DTAPDFTLPD ADGNDVALAD YRGRKVVVYF
YPAASTPGCT KQACDFRDNL AELNEAGIDV IGISPDKPAK LAKFRDNEEL TFPLLSDPER
ATLTAWGAFG EKTMYGKKVQ GVIRSTFLID ENGKVEVAQY NVRATGHVAK LRRDLSV
//
