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Protein

Alkyl hydroperoxide reductase subunit C

Gene

ahpC

Organism
Staphylococcus haemolyticus (strain JCSC1435)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei49 – 491Cysteine sulfenic acid (-SOH) intermediateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciSHAE279808:GJX7-2667-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Alkyl hydroperoxide reductase subunit C (EC:1.11.1.15)
Alternative name(s):
Peroxiredoxin
Thioredoxin peroxidase
Gene namesi
Name:ahpC
Ordered Locus Names:SH2592
OrganismiStaphylococcus haemolyticus (strain JCSC1435)
Taxonomic identifieri279808 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000543 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 189189Alkyl hydroperoxide reductase subunit CPRO_0000279761Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 – 49Interchain (with C-168); in linked formBy similarity
Disulfide bondi168 – 168Interchain (with C-49); in linked formBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation.By similarity

Protein-protein interaction databases

STRINGi279808.SH2592.

Structurei

3D structure databases

ProteinModelPortaliQ4L376.
SMRiQ4L376. Positions 2-168.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 159158ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the AhpC/TSA family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4105D3R. Bacteria.
COG0450. LUCA.
HOGENOMiHOG000022343.
KOiK03386.
OMAiTQHAPAF.
OrthoDBiPOG091H026G.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR017559. AhpC.
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR03137. AhpC. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4L376-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLINKEILP FIAQAYDPKK DEFKEVSQDD LKGSWSVVCF YPADFSFVCP
60 70 80 90 100
TELEDLQNQY DKLQDLGVNV FSVSTDTHFV HKAWHDHSDA ISKIQYQMIG
110 120 130 140 150
DPSQTITRNF DVLDEEAGLA QRGTFIIDPD GVVQAAEINA DGIGRDASTL
160 170 180
VNKIKAAQYV RQHPGEVCPA KWEEGSESLQ PGLDLVGKI
Length:189
Mass (Da):21,047
Last modified:August 2, 2005 - v1
Checksum:i2A1F87D0EFB461AF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE05901.1.
RefSeqiWP_011276838.1. NC_007168.1.

Genome annotation databases

EnsemblBacteriaiBAE05901; BAE05901; SH2592.
GeneIDi24246502.
KEGGisha:SH2592.
PATRICi19621277. VBIStaHae67511_2541.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE05901.1.
RefSeqiWP_011276838.1. NC_007168.1.

3D structure databases

ProteinModelPortaliQ4L376.
SMRiQ4L376. Positions 2-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi279808.SH2592.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAE05901; BAE05901; SH2592.
GeneIDi24246502.
KEGGisha:SH2592.
PATRICi19621277. VBIStaHae67511_2541.

Phylogenomic databases

eggNOGiENOG4105D3R. Bacteria.
COG0450. LUCA.
HOGENOMiHOG000022343.
KOiK03386.
OMAiTQHAPAF.
OrthoDBiPOG091H026G.

Enzyme and pathway databases

BioCyciSHAE279808:GJX7-2667-MONOMER.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR017559. AhpC.
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR03137. AhpC. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAHPC_STAHJ
AccessioniPrimary (citable) accession number: Q4L376
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: August 2, 2005
Last modified: September 7, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.