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)

B1LEP8

- PDXH_ECOSM

UniProt

B1LEP8 - PDXH_ECOSM

Protein

Pyridoxine/pyridoxamine 5'-phosphate oxidase

Gene

pdxH

Organism
Escherichia coli (strain SMS-3-5 / SECEC)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (29 Apr 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 sitei67 – 671FMNUniRule annotation
    Binding sitei70 – 701FMN; via amide nitrogenUniRule annotation
    Binding sitei72 – 721SubstrateUniRule annotation
    Binding sitei89 – 891FMNUniRule annotation
    Binding sitei129 – 1291SubstrateUniRule annotation
    Binding sitei133 – 1331SubstrateUniRule annotation
    Binding sitei137 – 1371SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi82 – 832FMNUniRule annotation
    Nucleotide bindingi146 – 1472FMNUniRule 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

    BioCyciECOL439855:GHHB-1559-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:EcSMS35_1561
    OrganismiEscherichia coli (strain SMS-3-5 / SECEC)
    Taxonomic identifieri439855 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000007011: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 218218Pyridoxine/pyridoxamine 5'-phosphate oxidasePRO_1000186314Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi439855.EcSMS35_1561.

    Structurei

    3D structure databases

    ProteinModelPortaliB1LEP8.
    SMRiB1LEP8. Positions 5-218.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni14 – 174Substrate bindingUniRule annotation
    Regioni197 – 1993Substrate 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.

    B1LEP8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDNDELQQI AHLRREYTKG GLRRRDLPAD PLTLFERWLS QACDAKLADP    50
    TAMVVATVDE HGQPYQRIVL LKHYDEKGMV FYTNLGSRKA HQIENNPRVS 100
    LLFPWHTLER QVMVIGKAER LSTLEVMKYF HSRPRDSQIG AWVSKQSSRI 150
    SARGILESKF LELKQKFQQG EVPLPSFWGG FRVSLEQIEF WQGGEHRLHD 200
    RFLYQRENDA WKIDRLAP 218
    Length:218
    Mass (Da):25,531
    Last modified:April 29, 2008 - v1
    Checksum:i00EC6482D7082E02
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000970 Genomic DNA. Translation: ACB15859.1.
    RefSeqiYP_001743616.1. NC_010498.1.

    Genome annotation databases

    EnsemblBacteriaiACB15859; ACB15859; EcSMS35_1561.
    GeneIDi6144638.
    KEGGiecm:EcSMS35_1561.
    PATRICi18431993. VBIEscCol6161_1719.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000970 Genomic DNA. Translation: ACB15859.1 .
    RefSeqi YP_001743616.1. NC_010498.1.

    3D structure databases

    ProteinModelPortali B1LEP8.
    SMRi B1LEP8. Positions 5-218.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 439855.EcSMS35_1561.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACB15859 ; ACB15859 ; EcSMS35_1561 .
    GeneIDi 6144638.
    KEGGi ecm:EcSMS35_1561.
    PATRICi 18431993. VBIEscCol6161_1719.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00190 ; UER00304 .
    UPA00190 ; UER00305 .
    BioCyci ECOL439855:GHHB-1559-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. "Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5."
      Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.
      J. Bacteriol. 190:6779-6794(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SMS-3-5 / SECEC.

    Entry informationi

    Entry nameiPDXH_ECOSM
    AccessioniPrimary (citable) accession number: B1LEP8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: April 29, 2008
    Last modified: October 1, 2014
    This is version 51 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