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Protein

Alkyl hydroperoxide reductase C

Gene

ahpC

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

Functioni

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Is the primary scavenger for endogenously generated hydrogen peroxides.1 Publication

Miscellaneous

The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by AhpF.By similarity

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei47Cysteine sulfenic acid (-SOH) intermediate1 Publication1

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 C (EC:1.11.1.151 Publication)
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

Keywords - Cellular componenti

Cytoplasm

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 CAdd BLAST186

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei17N6-acetyllysine1 Publication1
Disulfide bondi47Interchain (with C-166); in linked formCombined sources1 Publication
Modified residuei93N6-acetyllysine1 Publication1
Modified residuei153N6-acetyllysine1 Publication1
Disulfide bondi166Interchain (with C-47); in linked formCombined sources1 Publication
Modified residuei169N6-acetyllysine1 Publication1
Modified residuei171N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PaxDbiP0AE08.
PRIDEiP0AE08.

2D gel databases

SWISS-2DPAGEiP0AE08.

PTM databases

iPTMnetiP0AE08.

Expressioni

Inductioni

Repressed by sulfate or cysteine.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation. 5 homodimers assemble to form a ring-like decamer (PubMed:7499381).1 Publication

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. 36 interactors.
MINTiMINT-1241588.
STRINGi316385.ECDH10B_0674.

Structurei

Secondary structure

1187
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 17Combined sources6
Beta strandi20 – 25Combined sources6
Helixi26 – 29Combined sources4
Beta strandi32 – 38Combined sources7
Helixi49 – 56Combined sources8
Helixi58 – 63Combined sources6
Beta strandi66 – 74Combined sources9
Helixi76 – 85Combined sources10
Helixi87 – 90Combined sources4
Beta strandi94 – 98Combined sources5
Helixi103 – 107Combined sources5
Turni113 – 116Combined sources4
Beta strandi120 – 125Combined sources6
Beta strandi129 – 137Combined sources9
Helixi145 – 159Combined sources15
Beta strandi172 – 174Combined sources3

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

Keywords - Domaini

Redox-active center

Phylogenomic databases

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

Family and domain databases

InterProiView protein in InterPro
IPR017559. AhpC.
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR036249. Thioredoxin-like_sf.
IPR013766. Thioredoxin_domain.
PANTHERiPTHR10681:SF121. PTHR10681:SF121. 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.
PATRICifig|1411691.4.peg.1663.

Similar proteinsi

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: October 25, 2017
This is version 109 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