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P0A251

- AHPC_SALTY

UniProt

P0A251 - AHPC_SALTY

Protein

Alkyl hydroperoxide reductase subunit C

Gene

ahpC

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei47 – 471Cysteine sulfenic acid (-SOH) intermediate

    GO - Molecular functioni

    1. peroxidase activity Source: UniProtKB-KW
    2. peroxiredoxin activity Source: UniProtKB-EC

    GO - Biological processi

    1. response to oxidative stress Source: InterPro

    Keywords - Molecular functioni

    Antioxidant, Oxidoreductase, Peroxidase

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-611-MONOMER.

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000001014: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 187186Alkyl hydroperoxide reductase subunit CPRO_0000135120Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi47 – 47Interchain (with C-166); in linked form
    Disulfide bondi166 – 166Interchain (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

    1
    187
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 176
    Beta strandi20 – 256
    Helixi26 – 294
    Beta strandi32 – 387
    Beta strandi42 – 454
    Helixi46 – 5611
    Helixi58 – 636
    Beta strandi66 – 749
    Helixi76 – 8510
    Helixi89 – 913
    Beta strandi94 – 985
    Helixi103 – 1075
    Turni113 – 1153
    Beta strandi120 – 1256
    Beta strandi129 – 1379
    Helixi145 – 16016
    Turni182 – 1865

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP0A251.
    SMRiP0A251. Positions 2-169.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A251.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 157156ThioredoxinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the AhpC/TSA family.Curated
    Contains 1 thioredoxin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG0450.
    HOGENOMiHOG000022343.
    KOiK03386.
    OMAiPDEACPA.
    OrthoDBiEOG67X1XH.
    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.
    [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

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    MSLINTKIKP FKNQAFKNGE FIEVTEKDTE GRWSVFFFYP ADFTFVCPTE    50
    LGDVADHYEE LQKLGVDVYS VSTDTHFTHK AWHSSSETIA KIKYAMIGDP 100
    TGALTRNFDN MREDEGLADR ATFVVDPQGI IQAIEVTAEG IGRDASDLLR 150
    KIKAAQYVAA HPGEVCPAKW KEGEATLAPS LDLVGKI 187
    Length:187
    Mass (Da):20,747
    Last modified:January 23, 2007 - v2
    Checksum:i83B251C74DE9860D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21S → G AA sequence (PubMed:2643600)Curated
    Sequence conflicti5 – 51N → D AA sequence (PubMed:2643600)Curated
    Sequence conflicti14 – 141Q → N AA sequence (PubMed:2643600)Curated
    Sequence conflicti17 – 171K → H AA sequence (PubMed:2643600)Curated
    Sequence conflicti20 – 201E → H AA sequence (PubMed:2643600)Curated
    Sequence conflicti23 – 231E → S AA sequence (PubMed:2643600)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05478 Unassigned DNA. Translation: AAA16431.1.
    AE006468 Genomic DNA. Translation: AAL19559.1.
    PIRiA35441.
    RefSeqiNP_459600.1. NC_003197.1.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05478 Unassigned DNA. Translation: AAA16431.1 .
    AE006468 Genomic DNA. Translation: AAL19559.1 .
    PIRi A35441.
    RefSeqi NP_459600.1. NC_003197.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1N8J X-ray 2.17 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T 2-187 [» ]
    1YEP X-ray 2.50 A/B/C/D/E 2-187 [» ]
    1YEX X-ray 2.30 A/B/C/D/E 2-187 [» ]
    1YF0 X-ray 2.50 A/B/C/D/E 2-187 [» ]
    1YF1 X-ray 2.60 A/B/C/D/E/F/G/H/I/J 2-187 [» ]
    3EMP X-ray 4.00 A/B/C/D/E 2-187 [» ]
    4MA9 X-ray 1.82 A/B/C/D/E 2-187 [» ]
    4MAB X-ray 1.90 A/B/C/D/E 2-187 [» ]
    ProteinModelPortali P0A251.
    SMRi P0A251. Positions 2-169.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 99287.STM0608.

    Protein family/group databases

    PeroxiBasei 4829. SetypAhpC.

    Proteomic databases

    PaxDbi P0A251.
    PRIDEi P0A251.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL19559 ; AAL19559 ; STM0608 .
    GeneIDi 1252128.
    KEGGi stm:STM0608.
    PATRICi 32379561. VBISalEnt20916_0640.

    Phylogenomic databases

    eggNOGi COG0450.
    HOGENOMi HOG000022343.
    KOi K03386.
    OMAi PDEACPA.
    OrthoDBi EOG67X1XH.
    PhylomeDBi P0A251.

    Enzyme and pathway databases

    BioCyci SENT99287:GCTI-611-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A251.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR017559. AhpC.
    IPR000866. AhpC/TSA.
    IPR024706. Peroxiredoxin_AhpC-typ.
    IPR019479. Peroxiredoxin_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF10417. 1-cysPrx_C. 1 hit.
    PF00578. AhpC-TSA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000239. AHPC. 1 hit.
    SUPFAMi SSF52833. SSF52833. 1 hit.
    TIGRFAMsi TIGR03137. AhpC. 1 hit.
    PROSITEi PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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).

    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: October 1, 2014
    This is version 76 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

    External Data

    Dasty 3