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Protein

Alkyl hydroperoxide reductase subunit C

Gene

ahpC

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Directly reduces alkyl hydroperoxides with the use of electrons donated by the 57 kDa flavoprotein alkyl hydroperoxide reductase.

Catalytic activityi

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

Sites

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BRENDAi1.11.1.15. 5542.

Protein family/group databases

PeroxiBasei4829. SetypAhpC.

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
Thioredoxin peroxidase
Gene namesi
Name:ahpC
Ordered Locus Names:STM0608
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001351202 – 187Alkyl hydroperoxide reductase subunit CAdd BLAST186

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi47Interchain (with C-166); in linked form
Disulfide bondi166Interchain (with C-47); in linked form

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.

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP0A251.
PRIDEiP0A251.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation.

Protein-protein interaction databases

STRINGi99287.STM0608.

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
Beta strandi42 – 45Combined sources4
Helixi46 – 56Combined sources11
Helixi58 – 63Combined sources6
Beta strandi66 – 74Combined sources9
Helixi76 – 85Combined sources10
Helixi89 – 91Combined sources3
Beta strandi94 – 98Combined sources5
Helixi103 – 107Combined sources5
Turni113 – 115Combined sources3
Beta strandi116 – 118Combined sources3
Beta strandi120 – 125Combined sources6
Beta strandi129 – 137Combined sources9
Turni139 – 141Combined sources3
Helixi145 – 160Combined sources16
Beta strandi161 – 163Combined sources3
Turni182 – 186Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N8JX-ray2.17A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T2-187[»]
1YEPX-ray2.50A/B/C/D/E2-187[»]
1YEXX-ray2.30A/B/C/D/E2-187[»]
1YF0X-ray2.50A/B/C/D/E2-187[»]
1YF1X-ray2.60A/B/C/D/E/F/G/H/I/J2-187[»]
3EMPX-ray4.00A/B/C/D/E2-187[»]
4MA9X-ray1.82A/B/C/D/E2-187[»]
4MABX-ray1.90A/B/C/D/E2-187[»]
4XRAX-ray1.75A/B/C/D/E2-187[»]
4XRDX-ray2.30A/B/C/D/E2-187[»]
4XS1X-ray2.10A/B/C/D/E2-187[»]
4XS4X-ray2.65A/B/C/D/E2-187[»]
4XS6X-ray3.35A/B/C/D/E2-187[»]
4XS8X-ray1.90A/B/C/D/E2-187[»]
4XTSX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T2-187[»]
ProteinModelPortaliP0A251.
SMRiP0A251.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A251.

Family & Domainsi

Domains and Repeats

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

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.
OMAiAWHETSE.
PhylomeDBiP0A251.

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.

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

P0A251-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLINTKIKP FKNQAFKNGE FIEVTEKDTE GRWSVFFFYP ADFTFVCPTE
60 70 80 90 100
LGDVADHYEE LQKLGVDVYS VSTDTHFTHK AWHSSSETIA KIKYAMIGDP
110 120 130 140 150
TGALTRNFDN MREDEGLADR ATFVVDPQGI IQAIEVTAEG IGRDASDLLR
160 170 180
KIKAAQYVAA HPGEVCPAKW KEGEATLAPS LDLVGKI
Length:187
Mass (Da):20,747
Last modified:January 23, 2007 - v2
Checksum:i83B251C74DE9860D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2S → G AA sequence (PubMed:2643600).Curated1
Sequence conflicti5N → D AA sequence (PubMed:2643600).Curated1
Sequence conflicti14Q → N AA sequence (PubMed:2643600).Curated1
Sequence conflicti17K → H AA sequence (PubMed:2643600).Curated1
Sequence conflicti20E → H AA sequence (PubMed:2643600).Curated1
Sequence conflicti23E → S AA sequence (PubMed:2643600).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05478 Unassigned DNA. Translation: AAA16431.1.
AE006468 Genomic DNA. Translation: AAL19559.1.
PIRiA35441.
RefSeqiNP_459600.1. NC_003197.1.
WP_000052802.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL19559; AAL19559; STM0608.
GeneIDi1252128.
KEGGistm:STM0608.
PATRICi32379561. VBISalEnt20916_0640.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05478 Unassigned DNA. Translation: AAA16431.1.
AE006468 Genomic DNA. Translation: AAL19559.1.
PIRiA35441.
RefSeqiNP_459600.1. NC_003197.1.
WP_000052802.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N8JX-ray2.17A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T2-187[»]
1YEPX-ray2.50A/B/C/D/E2-187[»]
1YEXX-ray2.30A/B/C/D/E2-187[»]
1YF0X-ray2.50A/B/C/D/E2-187[»]
1YF1X-ray2.60A/B/C/D/E/F/G/H/I/J2-187[»]
3EMPX-ray4.00A/B/C/D/E2-187[»]
4MA9X-ray1.82A/B/C/D/E2-187[»]
4MABX-ray1.90A/B/C/D/E2-187[»]
4XRAX-ray1.75A/B/C/D/E2-187[»]
4XRDX-ray2.30A/B/C/D/E2-187[»]
4XS1X-ray2.10A/B/C/D/E2-187[»]
4XS4X-ray2.65A/B/C/D/E2-187[»]
4XS6X-ray3.35A/B/C/D/E2-187[»]
4XS8X-ray1.90A/B/C/D/E2-187[»]
4XTSX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T2-187[»]
ProteinModelPortaliP0A251.
SMRiP0A251.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM0608.

Protein family/group databases

PeroxiBasei4829. SetypAhpC.

Proteomic databases

PaxDbiP0A251.
PRIDEiP0A251.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL19559; AAL19559; STM0608.
GeneIDi1252128.
KEGGistm:STM0608.
PATRICi32379561. VBISalEnt20916_0640.

Phylogenomic databases

eggNOGiENOG4105D3R. Bacteria.
COG0450. LUCA.
HOGENOMiHOG000022343.
KOiK03386.
OMAiAWHETSE.
PhylomeDBiP0A251.

Enzyme and pathway databases

BRENDAi1.11.1.15. 5542.

Miscellaneous databases

EvolutionaryTraceiP0A251.

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_SALTY
AccessioniPrimary (citable) accession number: P0A251
Secondary accession number(s): P19479
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 91 of the entry and version 2 of the sequence. [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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.