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Protein

Hydroperoxy fatty acid reductase gpx2

Gene

gpx2

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hydroperoxy fatty acid reductase essential for the removal of lipid hydroperoxides under normal and stress conditions, leading to the protection of membrane integrity.1 Publication

Catalytic activityi

A hydroperoxy fatty acid + NADPH = a hydroxy fatty acid + NADP+ + H2O.1 Publication

Enzyme regulationi

Mercaptosuccinate, pCMB, and nethylmaleimide act as inhibitors of the catalytic activity.1 Publication

Kineticsi

  1. KM=57.3 µM for NADPH1 Publication
  2. KM=82.1 µM for alpha-linolenic acid hydroperoxide1 Publication

    pH dependencei

    Optimum pH is 8.2.1 Publication

    Temperature dependencei

    Optimum temperature is 37 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei34 – 341By similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17843.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hydroperoxy fatty acid reductase gpx2 (EC:1.11.1.22)
    Gene namesi
    Name:gpx2
    Ordered Locus Names:slr1992
    OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
    Taxonomic identifieri1111708 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
    Proteomesi
    • UP000001425 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 154154Hydroperoxy fatty acid reductase gpx2PRO_0000424245Add
    BLAST

    Expressioni

    Inductioni

    High light, methylviologen, and salt stress conditions increase the expression level.1 Publication

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    IntActiP73824. 8 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP73824.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutathione peroxidase family.Curated

    Phylogenomic databases

    HOGENOMiHOG000277053.
    InParanoidiP73824.
    KOiK00432.
    OMAiRSPLYQF.
    PhylomeDBiP73824.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR000889. Glutathione_peroxidase.
    IPR029759. GPX_AS.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PANTHERiPTHR11592. PTHR11592. 1 hit.
    PfamiPF00255. GSHPx. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
    PRINTSiPR01011. GLUTPROXDASE.
    SUPFAMiSSF52833. SSF52833. 1 hit.
    PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
    PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P73824-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPLPTSLTTL DGTPLAPEVI ADKVVLFVNV ASKCGLTPQY SGLVALDKAY
    60 70 80 90 100
    GEKGLVIIGV PCNQFGAQEP GSPEEIKDFT KTKYDVDFTL LEKQDVNGPN
    110 120 130 140 150
    RSPLYQFLVG DGEDISWNFG KFLIGRDGQV VARFDPQTKP DDTNLKAAIE

    KALG
    Length:154
    Mass (Da):16,646
    Last modified:February 1, 1997 - v1
    Checksum:i3758EF5DF85DEEB2
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000022 Genomic DNA. Translation: BAA17881.1.
    PIRiS75019.

    Genome annotation databases

    EnsemblBacteriaiBAA17881; BAA17881; BAA17881.
    KEGGisyn:slr1992.
    PATRICi23839725. VBISynSp132158_1424.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000022 Genomic DNA. Translation: BAA17881.1.
    PIRiS75019.

    3D structure databases

    ProteinModelPortaliP73824.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP73824. 8 interactions.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAA17881; BAA17881; BAA17881.
    KEGGisyn:slr1992.
    PATRICi23839725. VBISynSp132158_1424.

    Phylogenomic databases

    HOGENOMiHOG000277053.
    InParanoidiP73824.
    KOiK00432.
    OMAiRSPLYQF.
    PhylomeDBiP73824.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17843.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR000889. Glutathione_peroxidase.
    IPR029759. GPX_AS.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PANTHERiPTHR11592. PTHR11592. 1 hit.
    PfamiPF00255. GSHPx. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
    PRINTSiPR01011. GLUTPROXDASE.
    SUPFAMiSSF52833. SSF52833. 1 hit.
    PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
    PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
      Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.
      , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PCC 6803 / Kazusa.
    2. "NADPH-dependent glutathione peroxidase-like proteins (Gpx-1, Gpx-2) reduce unsaturated fatty acid hydroperoxides in Synechocystis PCC 6803."
      Gaber A., Tamoi M., Takeda T., Nakano Y., Shigeoka S.
      FEBS Lett. 499:32-36(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    3. "Induction and functional analysis of two reduced nicotinamide adenine dinucleotide phosphate-dependent glutathione peroxidase-like proteins in Synechocystis PCC 6803 during the progression of oxidative stress."
      Gaber A., Yoshimura K., Tamoi M., Takeda T., Nakano Y., Shigeoka S.
      Plant Physiol. 136:2855-2861(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, FUNCTION.

    Entry informationi

    Entry nameiGPX2_SYNY3
    AccessioniPrimary (citable) accession number: P73824
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2013
    Last sequence update: February 1, 1997
    Last modified: March 16, 2016
    This is version 108 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Synechocystis PCC 6803
      Synechocystis (strain PCC 6803): entries and gene names

    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.