(data stored in SCRATCH zone)

SWISSPROT: B1VRK9_STRGG

ID   B1VRK9_STRGG            Unreviewed;       182 AA.
AC   B1VRK9;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-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=SGR_598 {ECO:0000313|EMBL:BAG17427.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG17427.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG17427.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism
RT   Streptomyces griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
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; AP009493; BAG17427.1; -; Genomic_DNA.
DR   RefSeq; WP_012377917.1; NC_010572.1.
DR   STRING; 455632.SGR_598; -.
DR   EnsemblBacteria; BAG17427; BAG17427; SGR_598.
DR   GeneID; 6211124; -.
DR   KEGG; sgr:SGR_598; -.
DR   PATRIC; fig|455632.4.peg.581; -.
DR   eggNOG; ENOG4108T6S; Bacteria.
DR   eggNOG; COG2128; LUCA.
DR   HOGENOM; HOG000218410; -.
DR   OMA; CLSAHTY; -.
DR   OrthoDB; 1925754at2; -.
DR   BioCyc; SGRI455632:G1G2X-591-MONOMER; -.
DR   Proteomes; UP000001685; 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; B1VRK9.
DR   SWISS-2DPAGE; B1VRK9.
KW   Antioxidant {ECO:0000256|SAAS:SAAS00461132};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001685};
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       41    104       CMD. {ECO:0000259|Pfam:PF02627}.
SQ   SEQUENCE   182 AA;  19342 MW;  2B8B6F14102A2BF2 CRC64;
     MPRIPVHTVD SAPAPGGETL RRLEKRFGRV LNIHGGMAHS PVVLATYAAM STAIAEHGTF
     DARTREAIAL AVGAVDACAY CQSAHTVSAR AAGFTEEQTV AIRRGERGDD PKLDALVQVA
     REVAGEVGEA SDAAWDEAAA QGWTDTQLTE VFAHVAVNLY TNYFNHYVRT ELDVPAAPGL
     DG
//

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