(data stored in ACNUC1104 zone)

SWISSPROT: AHPD_STRCO

ID   AHPD_STRCO              Reviewed;         178 AA.
AC   Q7AKI6;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 82.
DE   RecName: Full=Alkyl hydroperoxide reductase AhpD {ECO:0000255|HAMAP-Rule:MF_01676};
DE            EC=1.11.1.15 {ECO:0000255|HAMAP-Rule:MF_01676};
DE   AltName: Full=Alkylhydroperoxidase AhpD {ECO:0000255|HAMAP-Rule:MF_01676};
GN   Name=ahpD {ECO:0000255|HAMAP-Rule:MF_01676}; OrderedLocusNames=SCO5031;
GN   ORFNames=SCK7.04c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Antioxidant protein with alkyl hydroperoxidase activity.
CC       Required for the reduction of the AhpC active site cysteine residues
CC       and for the regeneration of the AhpC enzyme activity.
CC       {ECO:0000255|HAMAP-Rule:MF_01676}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + a hydroperoxide = [protein]-disulfide + an
CC         alcohol + H2O; Xref=Rhea:RHEA:10008, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC         COMP:10594, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.15;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01676};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01676}.
CC   -!- SIMILARITY: Belongs to the AhpD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01676}.
DR   EMBL; AL939122; CAC05876.1; -; Genomic_DNA.
DR   RefSeq; NP_629183.1; NC_003888.3.
DR   RefSeq; WP_003973946.1; NC_003888.3.
DR   SMR; Q7AKI6; -.
DR   STRING; 100226.SCO5031; -.
DR   PeroxiBase; 4586; ScoAhpD.
DR   PRIDE; Q7AKI6; -.
DR   EnsemblBacteria; CAC05876; CAC05876; CAC05876.
DR   GeneID; 1100472; -.
DR   KEGG; sco:SCO5031; -.
DR   eggNOG; ENOG4108X7C; Bacteria.
DR   eggNOG; COG2128; LUCA.
DR   HOGENOM; HOG000261487; -.
DR   InParanoid; Q7AKI6; -.
DR   KO; K04756; -.
DR   OMA; AIMAMNN; -.
DR   PhylomeDB; Q7AKI6; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0008785; F:alkyl hydroperoxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032843; F:hydroperoxide reductase activity; IEA:InterPro.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 1.20.1290.10; -; 1.
DR   HAMAP; MF_01676; AhpD; 1.
DR   InterPro; IPR004674; AhpD.
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; TIGR00777; ahpD; 1.
DR   TIGRFAMs; TIGR00778; ahpD_dom; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7AKI6.
DR   SWISS-2DPAGE; Q7AKI6.
KW   Antioxidant; Disulfide bond; Oxidoreductase; Peroxidase;
KW   Redox-active center; Reference proteome.
FT   CHAIN           1..178
FT                   /note="Alkyl hydroperoxide reductase AhpD"
FT                   /id="PRO_0000359509"
FT   ACT_SITE        131
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01676"
FT   ACT_SITE        134
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01676"
FT   DISULFID        131..134
FT                   /evidence="ECO:0000250"
FT   DISULFID        134
FT                   /note="Interchain (with AhpC); in linked form"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01676"
SQ   SEQUENCE   178 AA;  19002 MW;  1CB543F2E1A33E2F CRC64;
     MSLDSLKSAV PDYAKDLKLN LGSVIGNSDL PAQQLWGTVL ATAIASRSPI VLRELEPEAK
     ANLSPEAYSA AKSAAAVMAM NNVFYRTRHL LSDHEYGTLR AGLRMNVIGN PGVDKVDFEL
     WSFAVSAING CGMCLDSHEQ VLRKAGVDRE TIQEAFKIAA VVEAVGVTLD AEAVLAAE
//

If you have problems or comments...

PBIL Back to PBIL home page