(data stored in SCRATCH zone)

SWISSPROT: Q13RV8_PARXL

ID   Q13RV8_PARXL            Unreviewed;       234 AA.
AC   Q13RV8;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 82.
DE   RecName: Full=Peroxiredoxin {ECO:0000256|HAMAP-Rule:MF_00401};
DE            EC=1.11.1.15 {ECO:0000256|HAMAP-Rule:MF_00401};
GN   ORFNames=Bxe_B2814 {ECO:0000313|EMBL:ABE33181.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33181.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33181.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33181.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
CC       of hydrogen peroxide and organic hydroperoxides to water and
CC       alcohols, respectively. Plays a role in cell protection against
CC       oxidative stress by detoxifying peroxides. {ECO:0000256|HAMAP-
CC       Rule:MF_00401}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + a hydroperoxide = [protein]-disulfide
CC         + an alcohol + H2O; Xref=Rhea:RHEA:10008, Rhea:RHEA-COMP:10593,
CC         Rhea:RHEA-COMP:10594, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058;
CC         EC=1.11.1.15; Evidence={ECO:0000256|HAMAP-Rule:MF_00401};
CC   -!- SUBUNIT: Homodecamer. Pentamer of dimers that assemble into a ring
CC       structure. {ECO:0000256|HAMAP-Rule:MF_00401}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00401}.
CC   -!- MISCELLANEOUS: The active site is a conserved redox-active
CC       cysteine residue, the peroxidatic cysteine (C(P)), which makes the
CC       nucleophilic attack on the peroxide substrate. The peroxide
CC       oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which
CC       then reacts with another cysteine residue, the resolving cysteine
CC       (C(R)), to form a disulfide bridge. The disulfide is subsequently
CC       reduced by an appropriate electron donor to complete the catalytic
CC       cycle. In this 1-Cys peroxiredoxin, no C(R) is present and C(P)
CC       instead forms a disulfide with a cysteine from another protein or
CC       with a small thiol molecule. {ECO:0000256|HAMAP-Rule:MF_00401}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00401}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00401}.
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DR   EMBL; CP000271; ABE33181.1; -; Genomic_DNA.
DR   RefSeq; WP_011490556.1; NZ_CP008762.1.
DR   STRING; 266265.Bxe_B2814; -.
DR   EnsemblBacteria; ABE33181; ABE33181; Bxe_B2814.
DR   GeneID; 4006587; -.
DR   KEGG; bxb:DR64_5143; -.
DR   KEGG; bxe:Bxe_B2814; -.
DR   PATRIC; fig|266265.5.peg.4879; -.
DR   eggNOG; ENOG4105D3R; Bacteria.
DR   eggNOG; COG0450; LUCA.
DR   HOGENOM; HOG000022346; -.
DR   KO; K03386; -.
DR   OMA; MVYYPMT; -.
DR   OrthoDB; 892697at2; -.
DR   BioCyc; BXEN266265:BXE_RS23140-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   HAMAP; MF_00401; Peroxiredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR022915; Peroxiredoxin_TDXH.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13RV8.
DR   SWISS-2DPAGE; Q13RV8.
KW   Antioxidant {ECO:0000256|HAMAP-Rule:MF_00401};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00401};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00401,
KW   ECO:0000313|EMBL:ABE33181.1};
KW   Peroxidase {ECO:0000256|HAMAP-Rule:MF_00401,
KW   ECO:0000313|EMBL:ABE33181.1};
KW   Redox-active center {ECO:0000256|HAMAP-Rule:MF_00401};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN       14    169       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
FT   ACT_SITE     55     55       Cysteine sulfenic acid (-SOH)
FT                                intermediate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00401, ECO:0000256|PIRSR:PIRSR000239-
FT                                1}.
FT   BINDING     132    132       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00401}.
SQ   SEQUENCE   234 AA;  26495 MW;  514266D1E5C86DC9 CRC64;
     MDNIEEDFRA QRPPFLYEPA PDFEARSTMG MVSSADYRGK WLLFFSHPAD FTPVCTSELI
     AFARIAPRFK ELGCELLALS IDGLYSHLAW LRSIQERFNM DIPFPVVEDP SMAVAKAYGM
     LPPKAVSSST VRGMFLIDPE GIIKAISWYP ISTGRSVEEA FRLFQAVRMT WQENLYAPAD
     WQPGSPCVVP PPKTIEDASK RLSEGDVLDW YYQTRQIAQD APPERAPVKR GRRA
//

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