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P21159

- PDXH_MYXXA

UniProt

P21159 - PDXH_MYXXA

Protein

Pyridoxine/pyridoxamine 5'-phosphate oxidase

Gene

pdxH

Organism
Myxococcus xanthus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 2 (24 Jan 2006)
      Previous versions | rss
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    • Comment

    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.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei69 – 691FMNUniRule annotation
    Binding sitei72 – 721FMN; via amide nitrogenUniRule annotation
    Binding sitei74 – 741SubstrateUniRule annotation
    Binding sitei91 – 911FMNUniRule annotation
    Binding sitei131 – 1311SubstrateUniRule annotation
    Binding sitei135 – 1351SubstrateUniRule annotation
    Binding sitei139 – 1391SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi84 – 852FMNUniRule annotation
    Nucleotide bindingi148 – 1492FMNUniRule 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

    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
    Synonyms:fprA
    OrganismiMyxococcus xanthus
    Taxonomic identifieri34 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeMyxococcus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 220220Pyridoxine/pyridoxamine 5'-phosphate oxidasePRO_0000167724Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliP21159.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni199 – 2013Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    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.

    P21159-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRTLTCVPDE STAKVHTCRA PFMLHRVMIP PDPIQRFAEL FERAKQAIAV    50
    DPNAMVVATV GDDGRPSARV VLLKDFDARG FVFYTNHESR KGREARAHPY 100
    AALCFYWQPL NEQVRVEGRV ERVTDAEADA YFQSRARGSQ VGAWASLQSQ 150
    PLATREELEA RVAEVEQKYA GQPVPRPPHW SGFRVVPDRI EFWHAQESRL 200
    HDRHVYLRED GGWRTQMLYP 220
    Length:220
    Mass (Da):25,285
    Last modified:January 24, 2006 - v2
    Checksum:i656A388822028C2D
    GO

    Sequence cautioni

    The sequence AAA25392.2 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27429 Genomic DNA. Translation: AAA25392.2. Different initiation.
    PIRiS36092.
    T10126.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27429 Genomic DNA. Translation: AAA25392.2 . Different initiation.
    PIRi S36092.
    T10126.

    3D structure databases

    ProteinModelPortali P21159.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00190 ; UER00304 .
    UPA00190 ; UER00305 .

    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. "Nucleotide sequence and transcriptional products of the csg locus of Myxococcus xanthus."
      Hagen T.J., Shimkets L.J.
      J. Bacteriol. 172:15-23(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The Myxococcus xanthus FprA protein causes increased flavin biosynthesis in Escherichia coli."
      Shimkets L.J.
      J. Bacteriol. 172:24-30(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FMN-BINDING.

    Entry informationi

    Entry nameiPDXH_MYXXA
    AccessioniPrimary (citable) accession number: P21159
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 90 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3