ID A0A674HVJ3_TAEGU Unreviewed; 196 AA. AC A0A674HVJ3; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 29-MAY-2024, entry version 18. DE RecName: Full=Peroxiredoxin-1 {ECO:0000256|PIRNR:PIRNR000239}; DE EC=1.11.1.24 {ECO:0000256|PIRNR:PIRNR000239}; GN Name=PRDX1 {ECO:0000313|Ensembl:ENSTGUP00000038589.1}; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae; OC Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000038589.1, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Ensembl:ENSTGUP00000038589.1, ECO:0000313|Proteomes:UP000007754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E., RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P., RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O., RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L., RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C., RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K., RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A., RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] {ECO:0000313|Ensembl:ENSTGUP00000038589.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2024) to UniProtKB. CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of CC hydrogen peroxide and organic hydroperoxides to water and alcohols, CC respectively. {ECO:0000256|PIRNR:PIRNR000239}. 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 ECO:0000256|PIRNR:PIRNR000239}; CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. CC {ECO:0000256|ARBA:ARBA00009796}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; A0A674HVJ3; -. DR Ensembl; ENSTGUT00000026874.1; ENSTGUP00000038589.1; ENSTGUG00000023194.1. DR GeneTree; ENSGT00940000154277; -. DR Proteomes; UP000007754; Chromosome 8. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:TreeGrafter. DR GO; GO:0045454; P:cell redox homeostasis; IEA:TreeGrafter. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:TreeGrafter. DR GO; GO:0045321; P:leukocyte activation; IEA:TreeGrafter. DR GO; GO:0019430; P:removal of superoxide radicals; IEA:TreeGrafter. DR CDD; cd03015; PRX_Typ2cys; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR000866; AhpC/TSA. DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ. DR InterPro; IPR019479; Peroxiredoxin_C. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR013766; Thioredoxin_domain. DR PANTHER; PTHR10681:SF111; PEROXIREDOXIN-1; 1. DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1. DR Pfam; PF10417; 1-cysPrx_C; 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 Antioxidant {ECO:0000256|ARBA:ARBA00022862, ECO:0000256|PIRNR:PIRNR000239}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000239}; KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR000239}; KW Redox-active center {ECO:0000256|ARBA:ARBA00023284, KW ECO:0000256|PIRNR:PIRNR000239}; KW Reference proteome {ECO:0000313|Proteomes:UP000007754}. FT DOMAIN 6..165 FT /note="Thioredoxin" FT /evidence="ECO:0000259|PROSITE:PS51352" FT REGION 174..196 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 182..196 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 52 FT /note="Cysteine sulfenic acid (-SOH) intermediate; for FT peroxidase activity" FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1" SQ SEQUENCE 196 AA; 21971 MW; ACD1FC6DCC21FA68 CRC64; MSSGKAFIGK PAPDFTATAV MPDGQFKDIK LSDYRGKYVV FFFYPLDFTF VCPTEIIAYS DRADEFKKIN CEVIGASVDS HFCHLAWINT PKKQGGLGTM KIPLISDTKR AIAKDYGVLK EDEGIAYRGL FIIDEKGILR QITINDLPVG RSVDETLRLV QAFQFTDKHG EAGWKPGSDT IKPDVQKSKE YFAKQK //