(data stored in SCRATCH zone)

SWISSPROT: C0ZNI8_RHOE4

ID   C0ZNI8_RHOE4            Unreviewed;       152 AA.
AC   C0ZNI8;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=Alkyl hydroperoxide reductase AhpD {ECO:0000256|SAAS:SAAS00088523};
DE            EC=1.11.1.15 {ECO:0000256|SAAS:SAAS00088503};
GN   OrderedLocusNames=RER_05320 {ECO:0000313|EMBL:BAH31240.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31240.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH31240.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus
RT   erythropolis strain PR4.";
RL   Environ. Microbiol. 8:334-346(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; AP008957; BAH31240.1; -; Genomic_DNA.
DR   RefSeq; WP_020905998.1; NC_012490.1.
DR   STRING; 234621.RER_05320; -.
DR   EnsemblBacteria; BAH31240; BAH31240; RER_05320.
DR   KEGG; rer:RER_05320; -.
DR   PATRIC; fig|234621.6.peg.975; -.
DR   eggNOG; ENOG4105MDH; Bacteria.
DR   eggNOG; COG2128; LUCA.
DR   HOGENOM; HOG000181201; -.
DR   OMA; LTINTWN; -.
DR   BioCyc; RERY234621:GHDE-549-MONOMER; -.
DR   Proteomes; UP000002204; 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; C0ZNI8.
DR   SWISS-2DPAGE; C0ZNI8.
KW   Antioxidant {ECO:0000256|SAAS:SAAS00461132};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002204};
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       16     97       CMD. {ECO:0000259|Pfam:PF02627}.
SQ   SEQUENCE   152 AA;  16895 MW;  D1DE65178DB49289 CRC64;
     MTTTTGQRLD IAKLAPEVYK AMIALDAAAR KGLEPTLVEL VLTRASQLNH CAWCLDMHTR
     DARKVGVTEQ KLYLLNAWEE ARGMYSDRER AALALTEAVT VLTDGFVPDE VYSEAAGEFS
     EEELAQLISV IFTINAWNRI AVTTRKAPPV RD
//

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