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
//