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)

Q9KKM4

- PDXH_VIBCH

UniProt

Q9KKM4 - PDXH_VIBCH

Protein

Pyridoxine/pyridoxamine 5'-phosphate oxidase

Gene

pdxH

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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 sitei60 – 601FMNUniRule annotation
    Binding sitei63 – 631FMN; via amide nitrogenUniRule annotation
    Binding sitei65 – 651SubstrateUniRule annotation
    Binding sitei82 – 821FMNUniRule annotation
    Binding sitei122 – 1221SubstrateUniRule annotation
    Binding sitei126 – 1261SubstrateUniRule annotation
    Binding sitei130 – 1301SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi75 – 762FMNUniRule annotation
    Nucleotide bindingi139 – 1402FMNUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. pyridoxal phosphate biosynthetic process Source: GOC
    2. pyridoxine biosynthetic process Source: TIGR

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Pyridoxine biosynthesis

    Keywords - Ligandi

    Flavoprotein, FMN

    Enzyme and pathway databases

    BioCyciVCHO:VCA1079-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:VC_A1079
    OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
    Taxonomic identifieri243277 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000000584: Chromosome 2

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 211211Pyridoxine/pyridoxamine 5'-phosphate oxidasePRO_0000167765Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi243277.VCA1079.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9KKM4.
    SMRiQ9KKM4. Positions 3-211.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni7 – 104Substrate bindingUniRule annotation
    Regioni190 – 1923Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0259.
    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.

    Q9KKM4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDLSDIRREY IHGGLRRKDL QANPIDQFNL WLQQAIDANL SDPTAMTVAT    50
    VDEHGQPFQR IVLLKNVDDA GFVFYTNLGS RKAQHIAHNN KISLHFPWHP 100
    LERQVHITGV AEKLTAMENM KYFMSRPKES QIAAIASHQS SRISARGVLE 150
    GKYLELKQKF ANGEIPVPSF WGGYRIRPES LEFWQGGEHR LHDRFLYSRQ 200
    DDNWTVDRLA P 211
    Length:211
    Mass (Da):24,363
    Last modified:October 1, 2000 - v1
    Checksum:i27A1B55B0DEE098E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE003853 Genomic DNA. Translation: AAF96972.1.
    PIRiC82381.
    RefSeqiNP_233460.1. NC_002506.1.

    Genome annotation databases

    EnsemblBacteriaiAAF96972; AAF96972; VC_A1079.
    GeneIDi2611970.
    KEGGivch:VCA1079.
    PATRICi20086674. VBIVibCho83274_3684.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE003853 Genomic DNA. Translation: AAF96972.1 .
    PIRi C82381.
    RefSeqi NP_233460.1. NC_002506.1.

    3D structure databases

    ProteinModelPortali Q9KKM4.
    SMRi Q9KKM4. Positions 3-211.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243277.VCA1079.

    Protocols and materials databases

    DNASUi 2611970.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF96972 ; AAF96972 ; VC_A1079 .
    GeneIDi 2611970.
    KEGGi vch:VCA1079.
    PATRICi 20086674. VBIVibCho83274_3684.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00190 ; UER00304 .
    UPA00190 ; UER00305 .
    BioCyci VCHO:VCA1079-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 39315 / El Tor Inaba N16961.

    Entry informationi

    Entry nameiPDXH_VIBCH
    AccessioniPrimary (citable) accession number: Q9KKM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 80 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3