ID A0A3Q4H453_NEOBR Unreviewed; 190 AA.
AC A0A3Q4H453;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Peroxiredoxin-5 {ECO:0000256|RuleBase:RU366011};
DE EC=1.11.1.24 {ECO:0000256|RuleBase:RU366011};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000016441.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000016441.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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|ARBA:ARBA00000280,
CC 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 RefSeq; XP_006799520.1; XM_006799457.1.
DR AlphaFoldDB; A0A3Q4H453; -.
DR STRING; 32507.ENSNBRP00000016441; -.
DR Ensembl; ENSNBRT00000016882.1; ENSNBRP00000016441.1; ENSNBRG00000012697.1.
DR GeneID; 102782363; -.
DR CTD; 25824; -.
DR GeneTree; ENSGT00390000018173; -.
DR OMA; PTCHSAH; -.
DR OrthoDB; 593245at2759; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000012697; Expressed in skeletal muscle tissue and 7 other cell types or tissues.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000261580}.
FT DOMAIN 31..190
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 75
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ SEQUENCE 190 AA; 20290 MW; 38D27C7AD9F5D1BB CRC64;
MLPVTSAVLR SSRVLQRARL LHITPTSKMP IQVGEHLPAV EVQEGEPGNK VAMDQLFKGK
KGVLFAVPGA FTPGCSKTHL PGFVEQAAEL KNKGIQEIAC ISVNDAFVMA AWGKEHGADG
KVRMLADPTG AFTKAVDLLL DIDQIVQVLG NKRSKRYSML VEDGVVKKLN VEPDGTGLTC
SLASSILSAE
//
