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P38013

- AHP1_YEAST

UniProt

P38013 - AHP1_YEAST

Protein

Peroxiredoxin type-2

Gene

AHP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Thiol-specific antioxidant protein with alkyl hydroperoxidase activity. Involved in osmotic stress resistance and detoxification of the cell. Preferentially eliminates organic peroxides rather than H2O2. Involved in cellular Mn2+ homeostasis.

    Catalytic activityi

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

    Kineticsi

    1. KM=150 µM for H2O21 Publication
    2. KM=45 µM for cumene hydroperoxide1 Publication
    3. KM=8 µM for tert-butyl hydroperoxide1 Publication
    4. KM=3 µM for TRX11 Publication
    5. KM=2 µM for TRX21 Publication

    Vmax=20 µmol/min/mg enzyme for H2O21 Publication

    Vmax=17 µmol/min/mg enzyme for cumene hydroperoxide1 Publication

    Vmax=14 µmol/min/mg enzyme for tert-butyl hydroperoxide1 Publication

    Vmax=17 µmol/min/mg enzyme for TRX11 Publication

    Vmax=16 µmol/min/mg enzyme for TRX21 Publication

    pH dependencei

    Optimum pH is 6.5.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei62 – 621Cysteine sulfenic acid (-SOH) intermediateSequence Analysis

    GO - Molecular functioni

    1. thioredoxin peroxidase activity Source: SGD

    GO - Biological processi

    1. cell redox homeostasis Source: SGD
    2. cellular response to oxidative stress Source: SGD
    3. response to metal ion Source: SGD

    Keywords - Molecular functioni

    Antioxidant, Oxidoreductase, Peroxidase

    Enzyme and pathway databases

    BioCyciYEAST:YLR109W-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxiredoxin type-2 (EC:1.11.1.15)
    Alternative name(s):
    AHPC1
    Cytoplasmic thiol peroxidase 3
    Short name:
    cTPx 3
    Peroxiredoxin type II
    Peroxisomal alkyl hydroperoxide reductase
    TPx type II
    Thiol-specific antioxidant II
    Short name:
    TSA II
    Thioredoxin peroxidase type II
    Thioredoxin reductase type II
    Gene namesi
    Name:AHP1
    Ordered Locus Names:YLR109W
    ORF Names:L2916, L9354.5
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    SGDiS000004099. AHP1.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 176175Peroxiredoxin type-2PRO_0000056610Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei28 – 281Phosphoserine1 Publication
    Modified residuei59 – 591Phosphoserine1 Publication
    Disulfide bondi62 – 62Interchain (with C-120); in linked form1 Publication
    Modified residuei116 – 1161Phosphoserine1 Publication
    Disulfide bondi120 – 120Interchain (with C-62); in linked form1 Publication

    Post-translational modificationi

    The Cys-62-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-62 (probably Cys-SOH) rapidly reacts with Cys-120-SH of the other subunit to form an intermolecular disulfide. This disulfide is subsequently reduced by thioredoxin to restore the reduced active form of the enzyme.
    Conjugated to URM1, a ubiquitin-like protein.

    Keywords - PTMi

    Acetylation, Disulfide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP38013.
    PaxDbiP38013.
    PeptideAtlasiP38013.

    2D gel databases

    COMPLUYEAST-2DPAGEP38013.

    Expressioni

    Inductioni

    By H2O2.1 Publication

    Gene expression databases

    GenevestigatoriP38013.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked, upon oxidation.1 Publication

    Protein-protein interaction databases

    BioGridi31382. 58 interactions.
    DIPiDIP-6375N.
    IntActiP38013. 4 interactions.
    MINTiMINT-705985.
    STRINGi4932.YLR109W.

    Structurei

    Secondary structure

    1
    176
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni3 – 64
    Beta strandi15 – 184
    Beta strandi23 – 253
    Helixi29 – 313
    Beta strandi35 – 384
    Helixi39 – 457
    Beta strandi47 – 537
    Helixi60 – 645
    Helixi67 – 8014
    Beta strandi85 – 928
    Helixi94 – 10310
    Beta strandi110 – 1167
    Helixi118 – 1203
    Helixi121 – 1255
    Beta strandi129 – 1335
    Beta strandi136 – 1394
    Beta strandi141 – 1477
    Beta strandi150 – 1567
    Turni160 – 1623
    Helixi169 – 1735

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4DSQX-ray2.40A/B/C/D1-176[»]
    4DSRX-ray2.91A/B/C/D1-176[»]
    4DSSX-ray2.10A1-176[»]
    4H86X-ray2.00A1-176[»]
    ProteinModelPortaliP38013.
    SMRiP38013. Positions 1-176.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 176168ThioredoxinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peroxiredoxin 2 family.Curated
    Contains 1 thioredoxin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG0678.
    GeneTreeiENSGT00390000018173.
    HOGENOMiHOG000255884.
    KOiK14171.
    OMAiCHANHAP.
    OrthoDBiEOG7X3R3F.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR013740. Redoxin.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF08534. Redoxin. 1 hit.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 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.

    P38013-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDLVNKKFP AGDYKFQYIA ISQSDADSES CKMPQTVEWS KLISENKKVI    50
    ITGAPAAFSP TCTVSHIPGY INYLDELVKE KEVDQVIVVT VDNPFANQAW 100
    AKSLGVKDTT HIKFASDPGC AFTKSIGFEL AVGDGVYWSG RWAMVVENGI 150
    VTYAAKETNP GTDVTVSSVE SVLAHL 176
    Length:176
    Mass (Da):19,115
    Last modified:January 23, 2007 - v4
    Checksum:i11B730781306A015
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 211I → T AA sequence (PubMed:9888818)Curated
    Sequence conflicti65 – 651S → V AA sequence (PubMed:9888818)Curated
    Sequence conflicti87 – 871I → E AA sequence (PubMed:9888818)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89514 Genomic DNA. Translation: CAA61687.1.
    Z73281 Genomic DNA. Translation: CAA97676.1.
    U53878 Genomic DNA. Translation: AAB67554.1.
    BK006945 Genomic DNA. Translation: DAA09425.1.
    PIRiS64946.
    RefSeqiNP_013210.1. NM_001181996.1.

    Genome annotation databases

    EnsemblFungiiYLR109W; YLR109W; YLR109W.
    GeneIDi850799.
    KEGGisce:YLR109W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89514 Genomic DNA. Translation: CAA61687.1 .
    Z73281 Genomic DNA. Translation: CAA97676.1 .
    U53878 Genomic DNA. Translation: AAB67554.1 .
    BK006945 Genomic DNA. Translation: DAA09425.1 .
    PIRi S64946.
    RefSeqi NP_013210.1. NM_001181996.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4DSQ X-ray 2.40 A/B/C/D 1-176 [» ]
    4DSR X-ray 2.91 A/B/C/D 1-176 [» ]
    4DSS X-ray 2.10 A 1-176 [» ]
    4H86 X-ray 2.00 A 1-176 [» ]
    ProteinModelPortali P38013.
    SMRi P38013. Positions 1-176.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31382. 58 interactions.
    DIPi DIP-6375N.
    IntActi P38013. 4 interactions.
    MINTi MINT-705985.
    STRINGi 4932.YLR109W.

    2D gel databases

    COMPLUYEAST-2DPAGE P38013.

    Proteomic databases

    MaxQBi P38013.
    PaxDbi P38013.
    PeptideAtlasi P38013.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR109W ; YLR109W ; YLR109W .
    GeneIDi 850799.
    KEGGi sce:YLR109W.

    Organism-specific databases

    SGDi S000004099. AHP1.

    Phylogenomic databases

    eggNOGi COG0678.
    GeneTreei ENSGT00390000018173.
    HOGENOMi HOG000255884.
    KOi K14171.
    OMAi CHANHAP.
    OrthoDBi EOG7X3R3F.

    Enzyme and pathway databases

    BioCyci YEAST:YLR109W-MONOMER.

    Miscellaneous databases

    NextBioi 967020.
    PROi P38013.

    Gene expression databases

    Genevestigatori P38013.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR013740. Redoxin.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF08534. Redoxin. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 1 hit.
    PROSITEi PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of a 37.6 kbp cosmid clone from the right arm of Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6, tRNA-Arg3 and 23 new open reading frames, among which several homologies to proteins involved in cell division control and to mammalian growth factors and other animal proteins are found."
      Verhasselt P., Volckaert G.
      Yeast 13:241-250(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 90840 / EAY235 / FY23.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Bienvenut W.V., Peters C.
      Submitted (MAY-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-8; 16-48; 80-102 AND 114-176, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    5. "Attachment of the ubiquitin-related protein Urm1p to the antioxidant protein Ahp1p."
      Goehring A.S., Rivers D.M., Sprague G.F. Jr.
      Eukaryot. Cell 2:930-936(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 8-15; 33-41; 80-102 AND 125-176, CONJUGATION TO URM1.
    6. "Purification and characterization of a second type thioredoxin peroxidase (type II TPx) from Saccharomyces cerevisiae."
      Jeong J.S., Kwon S.J., Kang S.W., Rhee S.G., Kim K.
      Biochemistry 38:776-783(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 16-41; 49-68; 82-96; 114-123 AND 142-150, POST-TRANSLATIONAL MODIFICATION, DISULFIDE BONDS, BIOPHYSICOCHEMICAL PROPERTIES.
    7. Cited for: PROTEIN SEQUENCE OF 82-99.
      Strain: ATCC 204508 / S288c.
    8. "A new antioxidant with alkyl hydroperoxide defense properties in yeast."
      Lee J., Spector D., Godon C., Labarre J., Toledano M.B.
      J. Biol. Chem. 274:4537-4544(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    9. "Involvement of thioredoxin peroxidase type II (Ahp1p) of Saccharomyces cerevisiae in Mn2+ homeostasis."
      Farcasanu I.C., Hirata D., Tsuchiya E., Mizuta K., Miyakawa T.
      Biosci. Biotechnol. Biochem. 63:1871-1881(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    10. "Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae."
      Park S.G., Cha M.-K., Jeong W., Kim I.-H.
      J. Biol. Chem. 275:5723-5732(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, INDUCTION, SUBCELLULAR LOCATION.
    11. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Characterization of the yeast peroxiredoxin Ahp1 in its reduced active and overoxidized inactive forms using NMR."
      Trivelli X., Krimm I., Ebel C., Verdoucq L., Prouzet-Mauleon V., Chartier Y., Tsan P., Lauquin G., Meyer Y., Lancelin J.-M.
      Biochemistry 42:14139-14149(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING, STRUCTURE BY NMR.
    15. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAHP1_YEAST
    AccessioniPrimary (citable) accession number: P38013
    Secondary accession number(s): D6VYA9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 148 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 16228 molecules/cell in log phase SD medium.1 Publication

    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
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3