ID A0A1B0B3D3_9MUSC Unreviewed; 187 AA.
AC A0A1B0B3D3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Peroxiredoxin-5 {ECO:0000256|RuleBase:RU366011};
DE EC=1.11.1.24 {ECO:0000256|RuleBase:RU366011};
OS Glossina palpalis gambiensis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=67801 {ECO:0000313|EnsemblMetazoa:GPPI017476-PA, ECO:0000313|Proteomes:UP000092460};
RN [1] {ECO:0000313|Proteomes:UP000092460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000092460};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GPPI017476-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPPI017476-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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|RuleBase:RU366011};
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix
CC {ECO:0000256|ARBA:ARBA00004253}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC {ECO:0000256|ARBA:ARBA00010505, ECO:0000256|RuleBase:RU366011}.
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DR EMBL; JXJN01007811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A1B0B3D3; -.
DR STRING; 67801.A0A1B0B3D3; -.
DR EnsemblMetazoa; GPPI017476-RA; GPPI017476-PA; GPPI017476.
DR VEuPathDB; VectorBase:GPPI017476; -.
DR Proteomes; UP000092460; Unassembled WGS sequence.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR CDD; cd03013; PRX5_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10430; PEROXIREDOXIN; 1.
DR PANTHER; PTHR10430:SF16; PEROXIREDOXIN-5, MITOCHONDRIAL; 1.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Antioxidant {ECO:0000256|RuleBase:RU366011};
KW Oxidoreductase {ECO:0000256|RuleBase:RU366011};
KW Peroxidase {ECO:0000256|RuleBase:RU366011};
KW Redox-active center {ECO:0000256|RuleBase:RU366011}.
FT DOMAIN 29..187
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 73
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ SEQUENCE 187 AA; 20618 MW; A356E4E7DA654404 CRC64;
MFLIRLLFQN CLMKGVTRRD FRTQRPAMAK VGDRLPSMAL FEDSLENEIN IRELTSNKKT
IIFGVHGAFT PDCSKIHLPG FVVSANYLKS ILNVHEIICI SVNDPFVMSV WGEEHGAGGR
IRMLADPSGD FVQVLDLAMN LPALGGLRSK RFSMIVGDTK VLKLNVEPDG TELGCSLAQN
IVKSGIN
//
