(data stored in ACNUC1104 zone)

SWISSPROT: C0ZNM4_RHOE4

ID   C0ZNM4_RHOE4            Unreviewed;       175 AA.
AC   C0ZNM4;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=Alkyl hydroperoxide reductase AhpD {ECO:0000256|SAAS:SAAS00088523};
DE            EC=1.11.1.15 {ECO:0000256|SAAS:SAAS00088503};
GN   OrderedLocusNames=RER_05680 {ECO:0000313|EMBL:BAH31276.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31276.1, 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:BAH31276.1, 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; AP008957; BAH31276.1; -; Genomic_DNA.
DR   RefSeq; WP_020906029.1; NC_012490.1.
DR   STRING; 234621.RER_05680; -.
DR   EnsemblBacteria; BAH31276; BAH31276; RER_05680.
DR   KEGG; rer:RER_05680; -.
DR   PATRIC; fig|234621.6.peg.1012; -.
DR   eggNOG; ENOG410810M; Bacteria.
DR   eggNOG; ENOG4111PXS; LUCA.
DR   HOGENOM; HOG000218410; -.
DR   OMA; NMLATFA; -.
DR   BioCyc; RERY234621:GHDE-585-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; C0ZNM4.
DR   SWISS-2DPAGE; C0ZNM4.
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       52    114       CMD. {ECO:0000259|Pfam:PF02627}.
SQ   SEQUENCE   175 AA;  18326 MW;  D35FA97D3B9199A0 CRC64;
     MSRLASLTPT TAVGASKDLL AELVNRHGQV GDMVAAMAHS PAVLGGYLQL SRAMKRAKLS
     RKITERISIA VQVQQGCAVC LEAHVAAAHA NGVEADEIER ARAGTSADPA IAAMIDLGLR
     VYREPASISD EHITGLRAHG YGDREIADVV GIVALNVLTG AFNLVAGVKP NEPDR
//

If you have problems or comments...

PBIL Back to PBIL home page