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P0A251 (AHPC_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alkyl hydroperoxide reductase subunit C

EC=1.11.1.15
Alternative name(s):
Alkyl hydroperoxide reductase protein C22
Peroxiredoxin
Thioredoxin peroxidase
Gene names
Name:ahpC
Ordered Locus Names:STM0608
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length187 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Subunit structure

Homodimer; disulfide-linked, upon oxidation.

Post-translational modification

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.

Sequence similarities

Belongs to the AhpC/TSA family.

Contains 1 thioredoxin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 187186Alkyl hydroperoxide reductase subunit C
PRO_0000135120

Regions

Domain2 – 157156Thioredoxin

Sites

Active site471Cysteine sulfenic acid (-SOH) intermediate

Amino acid modifications

Disulfide bond47Interchain (with C-166); in linked form
Disulfide bond166Interchain (with C-47); in linked form

Experimental info

Sequence conflict21S → G AA sequence Ref.4
Sequence conflict51N → D AA sequence Ref.4
Sequence conflict141Q → N AA sequence Ref.4
Sequence conflict171K → H AA sequence Ref.4
Sequence conflict201E → H AA sequence Ref.4
Sequence conflict231E → S AA sequence Ref.4

Secondary structure

................................. 187
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A251 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 83B251C74DE9860D

FASTA18720,747
        10         20         30         40         50         60 
MSLINTKIKP FKNQAFKNGE FIEVTEKDTE GRWSVFFFYP ADFTFVCPTE LGDVADHYEE 

        70         80         90        100        110        120 
LQKLGVDVYS VSTDTHFTHK AWHSSSETIA KIKYAMIGDP TGALTRNFDN MREDEGLADR 

       130        140        150        160        170        180 
ATFVVDPQGI IQAIEVTAEG IGRDASDLLR KIKAAQYVAA HPGEVCPAKW KEGEATLAPS 


LDLVGKI 

« Hide

References

« Hide 'large scale' references
[1]"Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and homology to thioredoxin reductase and other flavoprotein disulfide oxidoreductases."
Tartaglia L.A., Storz G., Brodsky M.H., Lai A., Ames B.N.
J. Biol. Chem. 265:10535-10540(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: TN1379.
[2]"Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes."
Chae H.Z., Robison K., Poole L.B., Church G., Storz G., Rhee S.G.
Proc. Natl. Acad. Sci. U.S.A. 91:7017-7021(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO C-TERMINUS.
[3]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[4]"An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage. Purification and properties."
Jacobson F.S., Morgan R.W., Christman M.F., Ames B.N.
J. Biol. Chem. 264:1488-1496(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-25.
Strain: oxyR1.
[5]"Identification and molecular analysis of oxyR-regulated promoters important for the bacterial adaptation to oxidative stress."
Tartaglia L.A., Storz G., Ames B.N.
J. Mol. Biol. 210:709-719(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[6]"Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins."
Wood Z.A., Poole L.B., Hantgan R.R., Karplus P.A.
Biochemistry 41:5493-5504(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[7]"Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling."
Wood Z.A., Poole L.B., Karplus P.A.
Science 300:650-653(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF MUTANT SER-47.
[8]"Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin."
Parsonage D., Youngblood D.S., Sarma G.N., Wood Z.A., Karplus P.A., Poole L.B.
Biochemistry 44:10583-10592(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05478 Unassigned DNA. Translation: AAA16431.1.
AE006468 Genomic DNA. Translation: AAL19559.1.
PIRA35441.
RefSeqNP_459600.1. NC_003197.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP0A251.
SMRP0A251. Positions 2-169.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM0608.

Protein family/group databases

PeroxiBase4829. SetypAhpC.

Proteomic databases

PaxDbP0A251.
PRIDEP0A251.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL19559; AAL19559; STM0608.
GeneID1252128.
KEGGstm:STM0608.
PATRIC32379561. VBISalEnt20916_0640.

Phylogenomic databases

eggNOGCOG0450.
HOGENOMHOG000022343.
KOK03386.
OMAPDEACPA.
OrthoDBEOG67X1XH.
PhylomeDBP0A251.

Enzyme and pathway databases

BioCycSENT99287:GCTI-611-MONOMER.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR017559. AhpC.
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFPIRSF000239. AHPC. 1 hit.
SUPFAMSSF52833. SSF52833. 1 hit.
TIGRFAMsTIGR03137. AhpC. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A251.

Entry information

Entry nameAHPC_SALTY
AccessionPrimary (citable) accession number: P0A251
Secondary accession number(s): P19479
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references