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Database: UniProt
Entry: A0A0E3UUB1_9FUSO
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ID   A0A0E3UUB1_9FUSO        Unreviewed;       152 AA.
AC   A0A0E3UUB1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=VC03_00795 {ECO:0000313|EMBL:AKC95128.1};
OS   Sneathia vaginalis.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Sneathia.
OX   NCBI_TaxID=187101 {ECO:0000313|EMBL:AKC95128.1, ECO:0000313|Proteomes:UP000033103};
RN   [1] {ECO:0000313|EMBL:AKC95128.1, ECO:0000313|Proteomes:UP000033103}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN35 {ECO:0000313|EMBL:AKC95128.1,
RC   ECO:0000313|Proteomes:UP000033103};
RX   PubMed=23281612;
RG   Vaginal Microbiome Consortium (additional members);
RA   Harwich M.D.Jr., Serrano M.G., Fettweis J.M., Alves J.M., Reimers M.A.,
RA   Buck G.A., Jefferson K.K.;
RT   "Genomic sequence analysis and characterization of Sneathia amnii sp.
RT   nov.";
RL   BMC Genomics 13:S4-S4(2012).
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; CP011280; AKC95128.1; -; Genomic_DNA.
DR   RefSeq; WP_046328234.1; NZ_CP011280.1.
DR   AlphaFoldDB; A0A0E3UUB1; -.
DR   STRING; 187101.VC03_00795; -.
DR   KEGG; sns:VC03_00795; -.
DR   PATRIC; fig|1069640.6.peg.151; -.
DR   HOGENOM; CLU_042529_14_1_0; -.
DR   OrthoDB; 9812811at2; -.
DR   Proteomes; UP000033103; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000033103}.
FT   DOMAIN          2..152
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   152 AA;  17866 MW;  8CEEF3A7BAD78544 CRC64;
     MINVGDVAYN FSLPDYTNTM YTLKQFRGKR VILYFYPKDD TIGCTQQACC YKKFYKEFLE
     LDVVLIGISI DSTESHAKFR NNFDLPFLLL SDSTKEVCEH YDVLKEKQMF GKKYIGVVRT
     TYIIDENGLV EKVYEKVNPR EDAEMVLKYL KK
//
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