(data stored in ACNUC7421 zone)

SWISSPROT: A0A0H2ZK86_PSEAB

ID   A0A0H2ZK86_PSEAB        Unreviewed;       145 AA.
AC   A0A0H2ZK86;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   08-MAY-2019, entry version 16.
DE   RecName: Full=Alkyl hydroperoxide reductase AhpD {ECO:0000256|SAAS:SAAS00088523};
DE            EC=1.11.1.15 {ECO:0000256|SAAS:SAAS00088503};
GN   OrderedLocusNames=PA14_03490 {ECO:0000313|EMBL:ABJ15232.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15232.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15232.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15232.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ15232.1; -; Genomic_DNA.
DR   RefSeq; WP_003084211.1; NC_008463.1.
DR   EnsemblBacteria; ABJ15232; ABJ15232; PA14_03490.
DR   KEGG; pau:PA14_03490; -.
DR   OMA; AINLWNR; -.
DR   BioCyc; PAER208963:G1G74-296-MONOMER; -.
DR   Proteomes; UP000000653; Chromosome.
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; A0A0H2ZK86.
DR   SWISS-2DPAGE; A0A0H2ZK86.
KW   Antioxidant {ECO:0000256|SAAS:SAAS00461132};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00461175};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS00461144};
KW   Peroxidase {ECO:0000256|SAAS:SAAS00461184};
KW   Redox-active center {ECO:0000256|SAAS:SAAS00461089}.
FT   DOMAIN       12     93       CMD. {ECO:0000259|Pfam:PF02627}.
SQ   SEQUENCE   145 AA;  16229 MW;  323BCBA790096419 CRC64;
     MTTRLEWAKA SPDAYAAMLG LEKALAKAGL ERPLIELVYL RTSQINGCAY CVNMHANDAR
     KAGETEQRLQ ALCVWQETPY FTPRERAALA WTEQLARLSQ GPLPHGLLDE LREHFDDKEI
     AELTLAVSAI NAWNRFGVGM GMQPE
//

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