Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A9QZ96

- PDXH_YERPG

UniProt

A9QZ96 - PDXH_YERPG

Protein

Pyridoxine/pyridoxamine 5'-phosphate oxidase

Gene

pdxH

Organism
Yersinia pestis bv. Antiqua (strain Angola)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (05 Feb 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • 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.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei66 – 661FMNUniRule annotation
    Binding sitei69 – 691FMN; via amide nitrogenUniRule annotation
    Binding sitei71 – 711SubstrateUniRule annotation
    Binding sitei88 – 881FMNUniRule annotation
    Binding sitei128 – 1281SubstrateUniRule annotation
    Binding sitei132 – 1321SubstrateUniRule annotation
    Binding sitei136 – 1361SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi81 – 822FMNUniRule annotation
    Nucleotide bindingi145 – 1462FMNUniRule 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

    BioCyciYPES349746:GHPB-2560-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:YpAngola_A2555
    OrganismiYersinia pestis bv. Antiqua (strain Angola)
    Taxonomic identifieri349746 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
    ProteomesiUP000001204: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 217217Pyridoxine/pyridoxamine 5'-phosphate oxidasePRO_1000186347Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi349746.YpAngola_A2555.

    Structurei

    3D structure databases

    ProteinModelPortaliA9QZ96.
    SMRiA9QZ96. Positions 9-217.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni13 – 164Substrate bindingUniRule annotation
    Regioni196 – 1983Substrate 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.

    A9QZ96-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTENNEFDVA DLRREYIRGG LRRSDLTENP LELFERWLKQ ACEARLPDPT    50
    AMCVATVDTN GQPYQRIVLL KHYDDQGLVF YTNLGSRKAQ QLAENPHISL 100
    LFPWHMLDRQ VIFLGKAERL STLEVLKYFH SRPKDSQIGA WVSQQSSRIS 150
    ARGVLESKFL ELKQKFQQGD VPLPSFWGGF RVKFDSVEFW QGGEHRLHDR 200
    FIYQREADAW KIDRLAP 217
    Length:217
    Mass (Da):25,383
    Last modified:February 5, 2008 - v1
    Checksum:i0CB7B6F07CB1DA86
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000901 Genomic DNA. Translation: ABX87086.1.
    RefSeqiYP_001606966.1. NC_010159.1.

    Genome annotation databases

    EnsemblBacteriaiABX87086; ABX87086; YpAngola_A2555.
    GeneIDi5801026.
    KEGGiypg:YpAngola_A2555.
    PATRICi18574537. VBIYerPes97331_3042.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000901 Genomic DNA. Translation: ABX87086.1 .
    RefSeqi YP_001606966.1. NC_010159.1.

    3D structure databases

    ProteinModelPortali A9QZ96.
    SMRi A9QZ96. Positions 9-217.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 349746.YpAngola_A2555.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABX87086 ; ABX87086 ; YpAngola_A2555 .
    GeneIDi 5801026.
    KEGGi ypg:YpAngola_A2555.
    PATRICi 18574537. VBIYerPes97331_3042.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00190 ; UER00304 .
    UPA00190 ; UER00305 .
    BioCyci YPES349746:GHPB-2560-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. "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium."
      Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J.
      J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Angola.

    Entry informationi

    Entry nameiPDXH_YERPG
    AccessioniPrimary (citable) accession number: A9QZ96
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 53 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