ID A0A0H5BBP2_BLAVI Unreviewed; 164 AA.
AC A0A0H5BBP2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin Bcp {ECO:0000256|ARBA:ARBA00042639};
GN Name=bcp {ECO:0000313|EMBL:CUU41574.1};
GN ORFNames=BV133_98 {ECO:0000313|EMBL:BAR97691.1}, BVIRIDIS_05670
GN {ECO:0000313|EMBL:CUU41574.1};
OS Blastochloris viridis (Rhodopseudomonas viridis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Blastochloridaceae; Blastochloris.
OX NCBI_TaxID=1079 {ECO:0000313|EMBL:CUU41574.1, ECO:0000313|Proteomes:UP000065734};
RN [1] {ECO:0000313|EMBL:BAR97691.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 133 {ECO:0000313|EMBL:BAR97691.1};
RA Tsukatani Y., Hirose Y., Harada J., Misawa N., Mori K., Inoue K.,
RA Tamiaki H.;
RT "Complete Genome Sequence of the Bacteriochlorophyll b-Producing
RT Photosynthetic Bacterium Blastochloris viridis.";
RL Genome Announc. 3:e01006-15(2015).
RN [2] {ECO:0000313|EMBL:CUU41574.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1 {ECO:0000313|EMBL:CUU41574.1};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000065734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19567 / DSM 133 / F {ECO:0000313|Proteomes:UP000065734};
RX PubMed=26798090; DOI=10.1128/genomeA.01520-15;
RA Liu L.N., Faulkner M., Liu X., Huang F., Darby A.C., Hall N.;
RT "Revised genome sequence of the purple photosynthetic bacterium
RT Blastochloris viridis.";
RL Genome Announc. 4:0-0(2016).
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; AP014854; BAR97691.1; -; Genomic_DNA.
DR EMBL; LN907867; CUU41574.1; -; Genomic_DNA.
DR RefSeq; WP_055036784.1; NZ_LN907867.1.
DR AlphaFoldDB; A0A0H5BBP2; -.
DR STRING; 1079.BVIR_1124; -.
DR KEGG; bvr:BVIR_1124; -.
DR PATRIC; fig|1079.6.peg.1165; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000065734; Chromosome I.
DR GO; GO:0004601; F:peroxidase 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; 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:CUU41574.1};
KW Peroxidase {ECO:0000313|EMBL:CUU41574.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000065734}.
FT DOMAIN 13..164
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 164 AA; 17056 MW; A931EDEFB1FB38C3 CRC64;
MVPTDSSTAP AALVVGEPAP AFDLPAAGGG RVSLASFAGK PLVVYFFPKA DTQGCTREAL
AFSALKPAFD RAGVAVIGVS ADPISRQDKF KAKHDLAVAL GSDETRAMVE AYGVWVEKSL
YGKTSMGIER ATVLIGPDGR VARVWRKVKV DGHADQVLAA ATAL
//