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Protein

Alkyl hydroperoxide reductase subunit C

Gene

ahpC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Directly reduces organic hydroperoxides in its reduced dithiol form.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei47Cysteine sulfenic acid (-SOH) intermediateBy similarity1

GO - Molecular functioni

  • hydroperoxide reductase activity Source: EcoliWiki
  • identical protein binding Source: IntAct
  • oxidoreductase activity, acting on peroxide as acceptor Source: EcoliWiki
  • peroxidase activity Source: EcoliWiki
  • peroxiredoxin activity Source: UniProtKB-EC

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • cellular response to sulfate starvation Source: EcoliWiki
  • iron assimilation by chelation and transport Source: CACAO
  • response to alkyl hydroperoxide Source: EcoCyc
  • response to hydroperoxide Source: EcoCyc

Keywordsi

Molecular functionAntioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciEcoCyc:EG11384-MONOMER.
MetaCyc:EG11384-MONOMER.
BRENDAi1.11.1.15. 2026.

Protein family/group databases

PeroxiBasei4830. EcoAhpC.

Names & Taxonomyi

Protein namesi
Recommended name:
Alkyl hydroperoxide reductase subunit C (EC:1.11.1.15)
Alternative name(s):
Alkyl hydroperoxide reductase protein C22
Peroxiredoxin
SCRP-23
Sulfate starvation-induced protein 8
Short name:
SSI8
Thioredoxin peroxidase
Gene namesi
Name:ahpC
Ordered Locus Names:b0605, JW0598
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11384. ahpC.

Subcellular locationi

GO - Cellular componenti

  • alkyl hydroperoxide reductase complex Source: EcoCyc
  • cytoplasm Source: EcoliWiki
  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB

Pathology & Biotechi

Disruption phenotypei

Increased sensitivity to hydroxyurea, probably because more reactive oxygen species accumulate.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved6 Publications
ChainiPRO_00001351152 – 187Alkyl hydroperoxide reductase subunit CAdd BLAST186

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei17N6-acetyllysine1 Publication1
Disulfide bondi47Interchain (with C-166); in linked formBy similarity
Modified residuei93N6-acetyllysine1 Publication1
Modified residuei153N6-acetyllysine1 Publication1
Disulfide bondi166Interchain (with C-47); in linked formBy similarity
Modified residuei169N6-acetyllysine1 Publication1
Modified residuei171N6-acetyllysine1 Publication1

Post-translational modificationi

The Cys-47-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-47 (probably Cys-SOH) rapidly reacts with Cys-166-SH of the other subunit to form an intermolecular disulfide. This disulfide is subsequently reduced by thioredoxin (By similarity).By similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

EPDiP0AE08.
PaxDbiP0AE08.
PRIDEiP0AE08.

2D gel databases

SWISS-2DPAGEP0AE08.

Expressioni

Inductioni

Repressed by sulfate or cysteine.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-547397,EBI-547397

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4259893. 12 interactors.
849610. 1 interactor.
DIPiDIP-36164N.
IntActiP0AE08. 33 interactors.
MINTiMINT-1241588.
STRINGi511145.b0605.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5B8AX-ray2.70A/B/C/D/E/F/G/H/I/J1-186[»]
5B8BX-ray3.10A/B/C/D/E/F/G/H/I/J1-186[»]
ProteinModelPortaliP0AE08.
SMRiP0AE08.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 157ThioredoxinPROSITE-ProRule annotationAdd BLAST156

Sequence similaritiesi

Belongs to the AhpC/TSA family.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4105D3R. Bacteria.
COG0450. LUCA.
HOGENOMiHOG000022343.
InParanoidiP0AE08.
KOiK03386.
OMAiAWHETSE.
PhylomeDBiP0AE08.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiView protein in InterPro
IPR017559. AhpC.
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
PANTHERiPTHR10681:SF128. PTHR10681:SF128. 1 hit.
PfamiView protein in Pfam
PF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR03137. AhpC. 1 hit.
PROSITEiView protein in PROSITE
PS51352. THIOREDOXIN_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AE08-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLINTKIKP FKNQAFKNGE FIEITEKDTE GRWSVFFFYP ADFTFVCPTE
60 70 80 90 100
LGDVADHYEE LQKLGVDVYA VSTDTHFTHK AWHSSSETIA KIKYAMIGDP
110 120 130 140 150
TGALTRNFDN MREDEGLADR ATFVVDPQGI IQAIEVTAEG IGRDASDLLR
160 170 180
KIKAAQYVAS HPGEVCPAKW KEGEATLAPS LDLVGKI
Length:187
Mass (Da):20,761
Last modified:January 23, 2007 - v2
Checksum:i40AB796E6F5CC2D6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13187 Genomic DNA. Translation: BAA02485.1.
U82598 Genomic DNA. Translation: AAB40806.1.
U00096 Genomic DNA. Translation: AAC73706.1.
AP009048 Genomic DNA. Translation: BAA35235.1.
PIRiC64794. JN0289.
RefSeqiNP_415138.1. NC_000913.3.
WP_000052796.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73706; AAC73706; b0605.
BAA35235; BAA35235; BAA35235.
GeneIDi945225.
KEGGiecj:JW0598.
eco:b0605.
PATRICi32116388. VBIEscCol129921_0634.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13187 Genomic DNA. Translation: BAA02485.1.
U82598 Genomic DNA. Translation: AAB40806.1.
U00096 Genomic DNA. Translation: AAC73706.1.
AP009048 Genomic DNA. Translation: BAA35235.1.
PIRiC64794. JN0289.
RefSeqiNP_415138.1. NC_000913.3.
WP_000052796.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5B8AX-ray2.70A/B/C/D/E/F/G/H/I/J1-186[»]
5B8BX-ray3.10A/B/C/D/E/F/G/H/I/J1-186[»]
ProteinModelPortaliP0AE08.
SMRiP0AE08.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259893. 12 interactors.
849610. 1 interactor.
DIPiDIP-36164N.
IntActiP0AE08. 33 interactors.
MINTiMINT-1241588.
STRINGi511145.b0605.

Protein family/group databases

PeroxiBasei4830. EcoAhpC.

2D gel databases

SWISS-2DPAGEP0AE08.

Proteomic databases

EPDiP0AE08.
PaxDbiP0AE08.
PRIDEiP0AE08.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73706; AAC73706; b0605.
BAA35235; BAA35235; BAA35235.
GeneIDi945225.
KEGGiecj:JW0598.
eco:b0605.
PATRICi32116388. VBIEscCol129921_0634.

Organism-specific databases

EchoBASEiEB1357.
EcoGeneiEG11384. ahpC.

Phylogenomic databases

eggNOGiENOG4105D3R. Bacteria.
COG0450. LUCA.
HOGENOMiHOG000022343.
InParanoidiP0AE08.
KOiK03386.
OMAiAWHETSE.
PhylomeDBiP0AE08.

Enzyme and pathway databases

BioCyciEcoCyc:EG11384-MONOMER.
MetaCyc:EG11384-MONOMER.
BRENDAi1.11.1.15. 2026.

Miscellaneous databases

PROiP0AE08.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiView protein in InterPro
IPR017559. AhpC.
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
PANTHERiPTHR10681:SF128. PTHR10681:SF128. 1 hit.
PfamiView protein in Pfam
PF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR03137. AhpC. 1 hit.
PROSITEiView protein in PROSITE
PS51352. THIOREDOXIN_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAHPC_ECOLI
AccessioniPrimary (citable) accession number: P0AE08
Secondary accession number(s): P26427
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: January 23, 2007
Last modified: March 15, 2017
This is version 103 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.