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Q5X7K4

- PDXH_LEGPA

UniProt

Q5X7K4 - PDXH_LEGPA

Protein

Pyridoxine/pyridoxamine 5'-phosphate oxidase

Gene

pdxH

Organism
Legionella pneumophila (strain Paris)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (23 Nov 2004)
      Previous versions | rss
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    Functioni

    Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).UniRule annotation

    Catalytic activityi

    Pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2.UniRule annotation
    Pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2.UniRule annotation

    Cofactori

    Binds 1 FMN per subunit.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei64 – 641FMNUniRule annotation
    Binding sitei67 – 671FMN; via amide nitrogenUniRule annotation
    Binding sitei69 – 691SubstrateUniRule annotation
    Binding sitei86 – 861FMNUniRule annotation
    Binding sitei126 – 1261SubstrateUniRule annotation
    Binding sitei130 – 1301SubstrateUniRule annotation
    Binding sitei134 – 1341SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi79 – 802FMNUniRule annotation
    Nucleotide bindingi143 – 1442FMNUniRule annotation

    GO - Molecular functioni

    1. FMN binding Source: UniProtKB-HAMAP
    2. pyridoxamine-phosphate oxidase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. pyridoxine biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Pyridoxine biosynthesis

    Keywords - Ligandi

    Flavoprotein, FMN

    Enzyme and pathway databases

    BioCyciLPNE297246:GCO9-783-MONOMER.
    UniPathwayiUPA00190; UER00304.
    UPA00190; UER00305.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyridoxine/pyridoxamine 5'-phosphate oxidaseUniRule annotation (EC:1.4.3.5UniRule annotation)
    Alternative name(s):
    PNP/PMP oxidaseUniRule annotation
    Short name:
    PNPOxUniRule annotation
    Pyridoxal 5'-phosphate synthaseUniRule annotation
    Gene namesi
    Name:pdxHUniRule annotation
    Ordered Locus Names:lpp0601
    OrganismiLegionella pneumophila (strain Paris)
    Taxonomic identifieri297246 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
    ProteomesiUP000000610: Chromosome

    Organism-specific databases

    LegioListilpp0601.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 215215Pyridoxine/pyridoxamine 5'-phosphate oxidasePRO_0000167715Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi297246.lpp0601.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5X7K4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni11 – 144Substrate bindingUniRule annotation
    Regioni194 – 1963Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the pyridoxamine 5'-phosphate oxidase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0259.
    HOGENOMiHOG000242755.
    KOiK00275.
    OMAiNMGSRKA.
    OrthoDBiEOG60KN2Z.

    Family and domain databases

    Gene3Di2.30.110.10. 1 hit.
    HAMAPiMF_01629. PdxH.
    InterProiIPR000659. Pyridox_Oxase.
    IPR019740. Pyridox_Oxase_CS.
    IPR011576. Pyridox_Oxase_FMN-bd.
    IPR019576. Pyridoxamine_oxidase_dimer_C.
    IPR012349. Split_barrel_FMN-bd.
    [Graphical view]
    PANTHERiPTHR10851. PTHR10851. 1 hit.
    PfamiPF10590. PNPOx_C. 1 hit.
    PF01243. Pyridox_oxidase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
    SUPFAMiSSF50475. SSF50475. 1 hit.
    TIGRFAMsiTIGR00558. pdxH. 1 hit.
    PROSITEiPS01064. PYRIDOX_OXIDASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5X7K4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKFRSLADI RRDYGELQLS EESAENDPIS QFKLWFDDVL LNEKNDPTAM    50
    VLSTVDEKGY PDSRVVLLKG LENGNFIFYT NYQSAKAMQI QKNPYAALNF 100
    YWPQMARQVR VRGRVKKISS EQSDAYFSSR PLKSQFSAIV SPQSQEILDR 150
    ISLEDALNQL IEEYGQKPVV RPENWGGYMI IPDEIEFWQG RDNRLHDRIH 200
    YYRHGHEWTH RRLAP 215
    Length:215
    Mass (Da):25,263
    Last modified:November 23, 2004 - v1
    Checksum:i86C5C8C6206BA2EC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR628336 Genomic DNA. Translation: CAH11749.1.
    RefSeqiYP_122939.1. NC_006368.1.

    Genome annotation databases

    EnsemblBacteriaiCAH11749; CAH11749; lpp0601.
    GeneIDi3119633.
    KEGGilpp:lpp0601.
    PATRICi22321436. VBILegPne27771_0789.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR628336 Genomic DNA. Translation: CAH11749.1 .
    RefSeqi YP_122939.1. NC_006368.1.

    3D structure databases

    ProteinModelPortali Q5X7K4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 297246.lpp0601.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAH11749 ; CAH11749 ; lpp0601 .
    GeneIDi 3119633.
    KEGGi lpp:lpp0601.
    PATRICi 22321436. VBILegPne27771_0789.

    Organism-specific databases

    LegioListi lpp0601.

    Phylogenomic databases

    eggNOGi COG0259.
    HOGENOMi HOG000242755.
    KOi K00275.
    OMAi NMGSRKA.
    OrthoDBi EOG60KN2Z.

    Enzyme and pathway databases

    UniPathwayi UPA00190 ; UER00304 .
    UPA00190 ; UER00305 .
    BioCyci LPNE297246:GCO9-783-MONOMER.

    Family and domain databases

    Gene3Di 2.30.110.10. 1 hit.
    HAMAPi MF_01629. PdxH.
    InterProi IPR000659. Pyridox_Oxase.
    IPR019740. Pyridox_Oxase_CS.
    IPR011576. Pyridox_Oxase_FMN-bd.
    IPR019576. Pyridoxamine_oxidase_dimer_C.
    IPR012349. Split_barrel_FMN-bd.
    [Graphical view ]
    PANTHERi PTHR10851. PTHR10851. 1 hit.
    Pfami PF10590. PNPOx_C. 1 hit.
    PF01243. Pyridox_oxidase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000190. Pyd_amn-ph_oxd. 1 hit.
    SUPFAMi SSF50475. SSF50475. 1 hit.
    TIGRFAMsi TIGR00558. pdxH. 1 hit.
    PROSITEi PS01064. PYRIDOX_OXIDASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
      Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
      Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Paris.

    Entry informationi

    Entry nameiPDXH_LEGPA
    AccessioniPrimary (citable) accession number: Q5X7K4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: November 23, 2004
    Last modified: October 1, 2014
    This is version 72 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3