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Reviewed, UniProtKB/Swiss-Prot Q5HRY1 (AHPC_STAEQ)

Last modified February 9, 2010. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alkyl hydroperoxide reductase subunit C
    EC=1.11.1.15
Alternative name(s):
    Peroxiredoxin
    Thioredoxin peroxidase
Gene names
Name: ahpC
Ordered Locus Names: SERP0060
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length189 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Directly reduces organic hydroperoxides in its reduced dithiol form By similarity.

Catalytic activity

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

Subunit structure

Homodimer; disulfide-linked, upon oxidation By similarity.

Post-translational modification

The Cys-49-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-49 (probably Cys-SOH) rapidly reacts with Cys-168-SH of the other subunit to form an intermolecular disulfide. This disulfide is subsequently reduced by thioredoxin By similarity.

Sequence similarities

Belongs to the ahpC/TSA family.

Contains 1 thioredoxin domain.

Ontologies

Keywords
   DomainRedox-active center
   Molecular functionAntioxidant
Oxidoreductase
Peroxidase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionperoxiredoxin activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 189189Alkyl hydroperoxide reductase subunit C
PRO_0000135130

Regions

Domain2 – 159158Thioredoxin

Sites

Active site491Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Disulfide bond49Interchain (with C-168); in linked form By similarity
Disulfide bond168Interchain (with C-49); in linked form By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HRY1-1 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 33183DA3D848D17F

FASTA18921,100
        10         20         30         40         50         60 
MSLINKEILP FTAQAYDPKK DEFKEVTQED FKGSWNVVCF YPADFSFVCP TELEDLQNQY 

        70         80         90        100        110        120 
AKLQELGVNV YSVSTDTHFV HKAWHDHSDA ISKLEYSMIG DPSQTITRNF DVLDEETGLA 

       130        140        150        160        170        180 
QRGTFIIDPD GVVQAAEINA DGIGRDASTL VNKIKAAQYV RQHPGEVCPA KWEEGSESLQ 


PGLDLVGKI 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000029 Genomic DNA. Translation: AAW53451.1.
RefSeqYP_187658.1.

3D structure databases

SMRQ5HRY1. Positions 2-168.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HRY1.

Genome annotation databases

GeneID3242975.
GenomeReviewsGene locus SERP0060 in contig CP000029_GR.
KEGGser:SERP0060.
NMPDRfig|176279.3.peg.289.
TIGRSERP0060.

Phylogenomic databases

eggNOGCOG0450.
HOGENOMHBG493509.
OMAGDLADHY.

Enzyme and pathway databases

BioCycSEPI176279:SERP0060-MONOMER.

Family and domain databases

InterProIPR000866. Alkyl_hydroperoxide_Rdtase.
IPR017559. Peroxiredoxin.
IPR017936. Thioredoxin-like.
IPR012336. Thioredoxin-like_fold.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF00578. AhpC-TSA. 1 hit.
[Graphical view]
TIGRFAMsTIGR03137. AhpC. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAHPC_STAEQ
AccessionPrimary (citable) accession number: Q5HRY1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: February 15, 2005
Last modified: February 9, 2010
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents