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Database: UniProt
Entry: A0A0U4VZL3_9PSED
LinkDB: A0A0U4VZL3_9PSED
Original site: A0A0U4VZL3_9PSED 
ID   A0A0U4VZL3_9PSED        Unreviewed;       187 AA.
AC   A0A0U4VZL3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Alkyl hydroperoxide reductase C {ECO:0000256|ARBA:ARBA00017462, ECO:0000256|RuleBase:RU366004};
DE            EC=1.11.1.26 {ECO:0000256|ARBA:ARBA00013021, ECO:0000256|RuleBase:RU366004};
DE   AltName: Full=Peroxiredoxin {ECO:0000256|ARBA:ARBA00032077, ECO:0000256|RuleBase:RU366004};
DE   AltName: Full=Thioredoxin peroxidase {ECO:0000256|ARBA:ARBA00032824, ECO:0000256|RuleBase:RU366004};
GN   ORFNames=APT59_10220 {ECO:0000313|EMBL:ALZ84552.1};
OS   Pseudomonas oryzihabitans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=47885 {ECO:0000313|EMBL:ALZ84552.1, ECO:0000313|Proteomes:UP000064137};
RN   [1] {ECO:0000313|EMBL:ALZ84552.1, ECO:0000313|Proteomes:UP000064137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USDA-ARS-USMARC-56511 {ECO:0000313|EMBL:ALZ84552.1,
RC   ECO:0000313|Proteomes:UP000064137};
RA   Harhay G.P., Harhay D.M., Smith T.P.L., Bono J.L., Heaton M.P.,
RA   Clawson M.L., Chitko-Mckown C.G., Capik S.F., DeDonder K.D., Apley M.D.,
RA   Lubbers B.V., White B.J., Larson R.L.;
RT   "Annotation of Pseudomonas oryzihabitans USDA-ARS-USMARC-56511.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|RuleBase:RU366004}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a hydroperoxide + H(+) + NADH = an alcohol + H2O + NAD(+);
CC         Xref=Rhea:RHEA:62628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.11.1.26;
CC         Evidence={ECO:0000256|ARBA:ARBA00000318,
CC         ECO:0000256|RuleBase:RU366004};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU366004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU366004}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009796, ECO:0000256|RuleBase:RU366004}.
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DR   EMBL; CP013987; ALZ84552.1; -; Genomic_DNA.
DR   RefSeq; WP_059314743.1; NZ_CP013987.1.
DR   AlphaFoldDB; A0A0U4VZL3; -.
DR   KEGG; por:APT59_10220; -.
DR   OrthoDB; 9812811at2; -.
DR   Proteomes; UP000064137; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0102039; F:NADH-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:UniProtKB-UniRule.
DR   CDD; cd03015; PRX_Typ2cys; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR017559; AhpC.
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   NCBIfam; TIGR03137; AhpC; 1.
DR   PANTHER; PTHR10681:SF121; ALKYL HYDROPEROXIDE REDUCTASE C; 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|RuleBase:RU366004};
KW   Cytoplasm {ECO:0000256|RuleBase:RU366004};
KW   Disulfide bond {ECO:0000256|RuleBase:RU366004};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU366004}; Peroxidase {ECO:0000256|RuleBase:RU366004};
KW   Redox-active center {ECO:0000256|RuleBase:RU366004};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064137}.
FT   DOMAIN          2..157
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        47
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT                   peroxidase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ   SEQUENCE   187 AA;  20778 MW;  F6C460AF859CF4AE CRC64;
     MSLINTEVKP FTATAYHNGK FVQVTEADLK GKWSAIVFYP ADFTFVCPTE LEDLADLYPE
     FQKLGVEIYG VSCDTHFAHK AWHDTSDAIK KVNYPLVGDP TARLARNFEV LIEEEGLALR
     GTFLINPEGQ IKLCEIHDNG IGRDASELLR KVRAAQYVAN HPGEVCPAKW KEGEATLTPS
     LDLVGKI
//
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