(data stored in SCRATCH zone)

SWISSPROT: B2JM04_PARP8

ID   B2JM04_PARP8            Unreviewed;       151 AA.
AC   B2JM04;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   RecName: Full=Alkyl hydroperoxide reductase AhpD {ECO:0000256|SAAS:SAAS00088523};
DE            EC=1.11.1.15 {ECO:0000256|SAAS:SAAS00088503};
GN   OrderedLocusNames=Bphy_3554 {ECO:0000313|EMBL:ACC72694.1};
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC72694.1, ECO:0000313|Proteomes:UP000001192};
RN   [1] {ECO:0000313|Proteomes:UP000001192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC   {ECO:0000313|Proteomes:UP000001192};
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A.,
RA   Melkonian R., James E.K., Young J.P., Bena G., Hauser L., Land M.,
RA   Kyrpides N., Bruce D., Chain P., Copeland A., Pitluck S., Woyke T.,
RA   Lizotte-Waniewski M., Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad
RT   host range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
CC   -!- FUNCTION: Antioxidant protein with alkyl hydroperoxidase activity.
CC       Required for the reduction of the AhpC active site cysteine
CC       residues and for the regeneration of the AhpC enzyme activity.
CC       {ECO:0000256|SAAS:SAAS00088543}.
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|SAAS:SAAS01124573};
CC   -!- SIMILARITY: Belongs to the AhpD family.
CC       {ECO:0000256|SAAS:SAAS00571262}.
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DR   EMBL; CP001044; ACC72694.1; -; Genomic_DNA.
DR   RefSeq; WP_012402867.1; NC_010623.1.
DR   STRING; 391038.Bphy_3554; -.
DR   EnsemblBacteria; ACC72694; ACC72694; Bphy_3554.
DR   GeneID; 27743225; -.
DR   KEGG; bph:Bphy_3554; -.
DR   eggNOG; ENOG4105MDH; Bacteria.
DR   eggNOG; COG2128; LUCA.
DR   HOGENOM; HOG000181201; -.
DR   OMA; GCSVCID; -.
DR   OrthoDB; 1893149at2; -.
DR   BioCyc; BPHY391038:G1GBS-3651-MONOMER; -.
DR   Proteomes; UP000001192; Chromosome 2.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.20.1290.10; -; 1.
DR   InterPro; IPR029032; AhpD-like.
DR   InterPro; IPR004675; AhpD_core.
DR   InterPro; IPR003779; CMD-like.
DR   Pfam; PF02627; CMD; 1.
DR   SUPFAM; SSF69118; SSF69118; 1.
DR   TIGRFAMs; TIGR00778; ahpD_dom; 1.
PE   3: Inferred from homology;
DR   PRODOM; B2JM04.
DR   SWISS-2DPAGE; B2JM04.
KW   Antioxidant {ECO:0000256|SAAS:SAAS00461132};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001192};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00461175};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS00461144};
KW   Peroxidase {ECO:0000256|SAAS:SAAS00461184,
KW   ECO:0000313|EMBL:ACC72694.1};
KW   Redox-active center {ECO:0000256|SAAS:SAAS00461089};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001192}.
FT   DOMAIN       16     94       CMD. {ECO:0000259|Pfam:PF02627}.
SQ   SEQUENCE   151 AA;  16752 MW;  F3426611A0914AA5 CRC64;
     MSKRLDYTQI APAGVKALGG VYGYVLQSGL SPVLVDLVYL RVSQINNCAY CLDMHTRDLL
     KKGVKVEKLA LVQAWREAGH LFDDRERAAL AWAESVTLVA QTGVPDEAYD AARAVFNDRE
     LVDLTIAISL MNTYNRMAIS FRNTPQAVME T
//

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