ID V6ITX7_9BACL Unreviewed; 155 AA.
AC V6ITX7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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 ORFNames=P343_18095 {ECO:0000313|EMBL:EST10280.1};
OS Sporolactobacillus laevolacticus DSM 442.
OC Bacteria; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC Sporolactobacillus.
OX NCBI_TaxID=1395513 {ECO:0000313|EMBL:EST10280.1, ECO:0000313|Proteomes:UP000018296};
RN [1] {ECO:0000313|EMBL:EST10280.1, ECO:0000313|Proteomes:UP000018296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 442 {ECO:0000313|EMBL:EST10280.1,
RC ECO:0000313|Proteomes:UP000018296};
RX PubMed=24371202;
RA Wang H., Wang L., Ju J., Yu B., Ma Y.;
RT "Genome Sequence of Sporolactobacillus laevolacticus DSM442, an Efficient
RT Polymer-Grade D-Lactate Producer from Agricultural Waste Cottonseed as a
RT Nitrogen Source.";
RL Genome Announc. 1:e01100-13(2013).
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}.
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:EST10280.1}.
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DR EMBL; AWTC01000028; EST10280.1; -; Genomic_DNA.
DR RefSeq; WP_023511793.1; NZ_AWTC01000028.1.
DR AlphaFoldDB; V6ITX7; -.
DR STRING; 1395513.P343_18095; -.
DR PATRIC; fig|1395513.3.peg.3660; -.
DR eggNOG; COG1225; Bacteria.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000018296; 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:SF24; PEROXIREDOXIN BCP; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000018296}.
FT DOMAIN 2..155
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 44
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 155 AA; 17418 MW; BB1239DF8AF07597 CRC64;
MLEAGTTAPE FTLKATEGNE VSLSDYKGKN VVLYFYPKDM TPGCTTEACD FRDQNSRFEE
LNTVVLGISP DPVEKHQKFT EKHTLPFTLL SDPEHAVAEQ YGSWQLKTTF GKKAMGIVRS
TFVINKEGII AQVWPKVKVA GHVDEVFQYV RENLA
//
