ID G2DVJ3_9GAMM Unreviewed; 154 AA.
AC G2DVJ3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
DE AltName: Full=Bacterioferritin comigratory protein {ECO:0000256|ARBA:ARBA00041373};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000256|ARBA:ARBA00032824};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin Q {ECO:0000256|ARBA:ARBA00042163};
GN ORFNames=ThidrDRAFT_0163 {ECO:0000313|EMBL:EGV34008.1};
OS Thiorhodococcus drewsii AZ1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiorhodococcus.
OX NCBI_TaxID=765913 {ECO:0000313|EMBL:EGV34008.1, ECO:0000313|Proteomes:UP000004200};
RN [1] {ECO:0000313|EMBL:EGV34008.1, ECO:0000313|Proteomes:UP000004200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ1 {ECO:0000313|EMBL:EGV34008.1,
RC ECO:0000313|Proteomes:UP000004200};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V.,
RA Frigaard N.-U., Bryant D.A., Woyke T.J.;
RT "The draft genome of Thiorhodococcus drewsii AZ1.";
RL Submitted (JUN-2011) 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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000256|ARBA:ARBA00004456}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC {ECO:0000256|ARBA:ARBA00038489}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGV34008.1}.
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DR EMBL; AFWT01000001; EGV34008.1; -; Genomic_DNA.
DR RefSeq; WP_007038879.1; NZ_AFWT01000001.1.
DR AlphaFoldDB; G2DVJ3; -.
DR STRING; 765913.ThidrDRAFT_0163; -.
DR PATRIC; fig|765913.3.peg.164; -.
DR eggNOG; COG1225; Bacteria.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000004200; Unassembled WGS sequence.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd03017; PRX_BCP; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR42801:SF4; AHPC_TSA FAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR42801; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078}.
FT DOMAIN 2..154
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 45
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 154 AA; 17279 MW; 9544A5CAEFB3B810 CRC64;
MLQPGDQAPL FSLPNADMER VSLEDLTHRR HCVIYFYPKD DTPGCTMEAL EFSDLQDDFE
AANTEIIGIS KDSCASHGAF RDKHGLSVQL LADTDGETCE AYGVWREKEA HGEKRMGIMR
STFVVDKDGL IRHALYDIKP KGHAARILDL IRAL
//
