ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P0A251


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name AHPC_SALTY
Primary accession number P0A251
Secondary accession number P19479
Integrated into Swiss-Prot on March 15, 2005
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 35)
Name and origin of the protein
Protein name Alkyl hydroperoxide reductase subunit C
Synonyms EC 1.11.1.15
Peroxiredoxin
Thioredoxin peroxidase
Alkyl hydroperoxide reductase protein C22
Gene name
Name: ahpC
OrderedLocusNames: STM0608
From
Salmonella typhimurium [TaxID: 602] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Salmonella.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=TN1379;
PubMed=2191951 [NCBI, ExPASy, EBI, Israel, Japan]
Tartaglia L.A., Storz G., Brodsky M.H., Lai A., Ames B.N.;
"Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and homology to thioredoxin reductase and other flavoprotein disulfide oxidoreductases.";
J. Biol. Chem. 265:10535-10540(1990).
[2]
SEQUENCE REVISION TO C-TERMINUS.
PubMed=8041738 [NCBI, ExPASy, EBI, Israel, Japan]
Chae H.Z., Robison K., Poole L.B., Church G., Storz G., Rhee S.G.;
"Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes.";
Proc. Natl. Acad. Sci. U.S.A. 91:7017-7021(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LT2 / SGSC1412 / ATCC 700720;
DOI=10.1038/35101614; PubMed=11677609 [NCBI, ExPASy, EBI, Israel, Japan]
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., Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.;
"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
Nature 413:852-856(2001).
[4]
PROTEIN SEQUENCE OF 2-25.
STRAIN=oxyR1;
PubMed=2643600 [NCBI, ExPASy, EBI, Israel, Japan]
Jacobson F.S., Morgan R.W., Christman M.F., Ames B.N.;
"An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage. Purification and properties.";
J. Biol. Chem. 264:1488-1496(1989).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
DOI=10.1016/0022-2836(89)90104-6; PubMed=2693740 [NCBI, ExPASy, EBI, Israel, Japan]
Tartaglia L.A., Storz G., Ames B.N.;
"Identification and molecular analysis of oxyR-regulated promoters important for the bacterial adaptation to oxidative stress.";
J. Mol. Biol. 210:709-719(1989).
[6]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1021/bi012173m; PubMed=11969410 [NCBI, ExPASy, EBI, Israel, Japan]
Wood Z.A., Poole L.B., Hantgan R.R., Karplus P.A.;
"Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins.";
Biochemistry 41:5493-5504(2002).
[7]
X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF MUTANT SER-47.
DOI=10.1126/science.1080405; PubMed=12714747 [NCBI, ExPASy, EBI, Israel, Japan]
Wood Z.A., Poole L.B., Karplus P.A.;
"Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling.";
Science 300:650-653(2003).
[8]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1021/bi050448i; PubMed=16060667 [NCBI, ExPASy, EBI, Israel, Japan]
Parsonage D., Youngblood D.S., Sarma G.N., Wood Z.A., Karplus P.A., Poole L.B.;
"Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin.";
Biochemistry 44:10583-10592(2005).
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: Homodimer; disulfide-linked, upon oxidation.
  • PTM: The Cys-47-SH group is the primary site of oxidation by H(2)O(2), 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.
  • SIMILARITY: Belongs to the ahpC/TSA family.
  • SIMILARITY: Contains 1 thioredoxin domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J05478; AAA16431.1; -; Unassigned_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE008724; AAL19559.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A35441; A35441.
RefSeq NP_459600.1; -.
3D structure databases
PDB
1N8J; X-ray; 2.17 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q=1-187, R/S/T=2-187.[ExPASy / RCSB / EBI]
1YEP; X-ray; 2.50 A; A/B/C/D/E=1-187.[ExPASy / RCSB / EBI]
1YEX; X-ray; 2.30 A; A/B/C/D/E=1-187.[ExPASy / RCSB / EBI]
1YF0; X-ray; 2.50 A; A/B/C/D/E=1-187.[ExPASy / RCSB / EBI]
1YF1; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J=1-187.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1N8J; -.
1YEP; -.
1YEX; -.
1YF0; -.
1YF1; -.
ModBase P0A251.
Protein family/group databases
PeroxiBase 4829; SetypAhpC.
Enzyme and pathway databases
BioCyc STYP99287:STM0608-MON; -.
Organism-specific databases
StyGene SG10004; ahpC.
Ontologies
GO
GO:0051920; Molecular function: peroxiredoxin activity (inferred from electronic annotation from EC).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000866; AhpC-TSA.
IPR017559; Peroxiredoxin.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
Pfam PF00578; AhpC-TSA; 1.
Pfam graphical view of domain structure.
PROSITE PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE P0A251; -.
Genome annotation databases
GeneID 1252128; -.
GenomeReviews AE006468_GR; STM0608.
KEGG stm:STM0608; -.
Phylogenomic databases
HOGENOM P0A251; -.
Other
LinkHub P0A251; -.
Genome annotation databases
CMR P0A251; STM0608.
Other
ProtoNet P0A251.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Antioxidant; Complete proteome; Direct protein sequencing; Oxidoreductase; Peroxidase; Redox-active center.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   187  186     Alkyl hydroperoxide reductase subunit C. PRO_0000135120
DOMAIN   2   157  156     Thioredoxin. 
ACT_SITE   47    47        Cysteine sulfenic acid (-SOH) intermediate. 
DISULFID   47    47        Interchain (with C-166); in linked form. 
DISULFID   166   166        Interchain (with C-47); in linked form. 
CONFLICT   2     2        S -> G (in Ref. 4; AA sequence). 
CONFLICT   5     5        N -> D (in Ref. 4; AA sequence). 
CONFLICT   14    14        Q -> N (in Ref. 4; AA sequence). 
CONFLICT   17    17        K -> H (in Ref. 4; AA sequence). 
CONFLICT   20    20        E -> H (in Ref. 4; AA sequence). 
CONFLICT   23    23        E -> S (in Ref. 4; AA sequence). 
STRAND   12    17  6      
STRAND   20    25  6      
HELIX   26    29  4      
STRAND   32    38  7      
HELIX   46    63  18      
STRAND   66    74  9      
HELIX   76    85  10      
HELIX   89    91  3      
STRAND   94    98  5      
HELIX   103   107  5      
TURN   113   115  3      
STRAND   120   125  6      
STRAND   129   137  9      
HELIX   145   160  16      
TURN   182   186  5      
Sequence information
Length: 187 AA [This is the length of the unprocessed precursor] Molecular weight: 20747 Da [This is the MW of the unprocessed precursor] CRC64: 83B251C74DE9860D [This is a checksum on the sequence]
        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 

P0A251 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!