Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Pyridoxine/pyridoxamine 5'-phosphate oxidase

Gene

pdxH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).3 Publications

Miscellaneous

Can bind a second molecule of pyridoxamine 5'-phosphate at a non-catalytic site in a cleft at the protein surface.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FMN6 PublicationsNote: Binds 1 FMN per subunit.6 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Kcat is 0.3 sec(-1) for oxidase activity with pyridoxine 5'-phosphate as substrate (at pH 7.6 and 37 degrees Celsius).1 Publication
  1. KM=0.3 µM for pyridoxamine 5'-phosphate1 Publication
  2. KM=2 µM for pyridoxine 5'-phosphate (at pH 7.6 and 37 degrees Celsius)2 Publications
  3. KM=105 µM for pyridoxamine 5'-phosphate (at pH 7.6 and 37 degrees Celsius)1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: pyridoxal 5'-phosphate salvage

    This protein is involved in step 1 of the subpathway that synthesizes pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate.
    Proteins known to be involved in this subpathway in this organism are:
    1. Pyridoxine/pyridoxamine 5'-phosphate oxidase (pdxH)
    This subpathway is part of the pathway pyridoxal 5'-phosphate salvage, which is itself part of Cofactor metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate, the pathway pyridoxal 5'-phosphate salvage and in Cofactor metabolism.

    Pathwayi: pyridoxal 5'-phosphate salvage

    This protein is involved in step 1 of the subpathway that synthesizes pyridoxal 5'-phosphate from pyridoxine 5'-phosphate.
    Proteins known to be involved in this subpathway in this organism are:
    1. Pyridoxine/pyridoxamine 5'-phosphate oxidase (pdxH)
    This subpathway is part of the pathway pyridoxal 5'-phosphate salvage, which is itself part of Cofactor metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyridoxal 5'-phosphate from pyridoxine 5'-phosphate, the pathway pyridoxal 5'-phosphate salvage and in Cofactor metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei72Substrate1 Publication1
    Binding sitei88FMN3 Publications1
    Binding sitei89FMN3 Publications1
    Binding sitei111FMN2 Publications1
    Binding sitei129Substrate1 Publication1
    Binding sitei133Substrate1 Publication1
    Binding sitei137Substrate1 Publication1
    Binding sitei191FMN1 Publication1
    Binding sitei201FMN2 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi67 – 72FMN3 Publications6
    Nucleotide bindingi82 – 83FMN3 Publications2
    Nucleotide bindingi146 – 147FMN3 Publications2

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionOxidoreductase
    Biological processPyridoxine biosynthesis
    LigandFlavoprotein, FMN

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:PDXH-MONOMER
    MetaCyc:PDXH-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.4.3.5 2026

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA01068;UER00304

    UPA01068;UER00305

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Pyridoxine/pyridoxamine 5'-phosphate oxidase (EC:1.4.3.53 Publications)
    Alternative name(s):
    PNP/PMP oxidase
    Short name:
    PNPOx
    Pyridoxal 5'-phosphate synthase
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:pdxH
    Ordered Locus Names:b1638, JW1630
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...
    EcoGenei
    EG11487 pdxH

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi14R → E: Reduces affinity for substrate about 7-fold, but has no effect on catalytic activity. 1 Publication1
    Mutagenesisi14R → M: Reduces affinity for substrate about 9-fold, but has no effect on catalytic activity. 1 Publication1
    Mutagenesisi17Y → F: Reduces affinity for substrate 3-fold, but has about 5-fold increase in catalytic activity. 1 Publication1
    Mutagenesisi49D → A: Reduces affinity for substrate 3-fold and catalytic activity 2-fold. 1 Publication1
    Mutagenesisi197R → E: Reduces affinity for substrate 8000-fold and catalytic activity 16-fold. 1 Publication1
    Mutagenesisi197R → M: Reduces affinity for substrate 300-fold and catalytic activity about 4-fold. 1 Publication1
    Mutagenesisi199H → A: Reduces affinity for substrate 230-fold, but has no effect on catalytic activity. 1 Publication1
    Mutagenesisi199H → N: Reduces catalytic activity about 4-fold, but has no effect on affinity for substrate. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB03345 Beta-Mercaptoethanol
    DB03247 Riboflavin Monophosphate

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001677062 – 218Pyridoxine/pyridoxamine 5'-phosphate oxidaseAdd BLAST217

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P0AFI7

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P0AFI7

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0AFI7

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.6 Publications

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4263488, 16 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-48024N

    Protein interaction database and analysis system

    More...
    IntActi
    P0AFI7, 13 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    316385.ECDH10B_1772

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1218
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P0AFI7

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P0AFI7

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P0AFI7

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni14 – 17Substrate binding1 Publication4
    Regioni197 – 199Substrate binding1 Publication3

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4108S7T Bacteria
    COG0259 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000242755

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0AFI7

    KEGG Orthology (KO)

    More...
    KOi
    K00275

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0AFI7

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.30.110.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01629 PdxH, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR000659 Pyridox_Oxase
    IPR019740 Pyridox_Oxase_CS
    IPR011576 Pyridox_Oxase_put
    IPR019576 Pyridoxamine_oxidase_dimer_C
    IPR012349 Split_barrel_FMN-bd

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR10851 PTHR10851, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF10590 PNP_phzG_C, 1 hit
    PF01243 Putative_PNPOx, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000190 Pyd_amn-ph_oxd, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00558 pdxH, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS01064 PYRIDOX_OXIDASE, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P0AFI7-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSDNDELQQI AHLRREYTKG GLRRRDLPAD PLTLFERWLS QACEAKLADP
    60 70 80 90 100
    TAMVVATVDE HGQPYQRIVL LKHYDEKGMV FYTNLGSRKA HQIENNPRVS
    110 120 130 140 150
    LLFPWHTLER QVMVIGKAER LSTLEVMKYF HSRPRDSQIG AWVSKQSSRI
    160 170 180 190 200
    SARGILESKF LELKQKFQQG EVPLPSFWGG FRVSLEQIEF WQGGEHRLHD
    210
    RFLYQRENDA WKIDRLAP
    Length:218
    Mass (Da):25,545
    Last modified:January 23, 2007 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8B47CEEEA6CEF5F9
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    M92351 Genomic DNA Translation: AAA24709.1
    U00096 Genomic DNA Translation: AAC74710.1
    AP009048 Genomic DNA Translation: BAA15399.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    B43261

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_416155.1, NC_000913.3
    WP_001282319.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC74710; AAC74710; b1638
    BAA15399; BAA15399; BAA15399

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    946806

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW1630
    eco:b1638

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.622

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M92351 Genomic DNA Translation: AAA24709.1
    U00096 Genomic DNA Translation: AAC74710.1
    AP009048 Genomic DNA Translation: BAA15399.1
    PIRiB43261
    RefSeqiNP_416155.1, NC_000913.3
    WP_001282319.1, NZ_LN832404.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1DNLX-ray1.80A20-218[»]
    1G76X-ray2.20A1-218[»]
    1G77X-ray2.10A1-218[»]
    1G78X-ray2.20A1-218[»]
    1G79X-ray2.00A1-218[»]
    1JNWX-ray2.07A1-218[»]
    1WV4X-ray2.60A/B1-218[»]
    ProteinModelPortaliP0AFI7
    SMRiP0AFI7
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4263488, 16 interactors
    DIPiDIP-48024N
    IntActiP0AFI7, 13 interactors
    STRINGi316385.ECDH10B_1772

    Chemistry databases

    DrugBankiDB03345 Beta-Mercaptoethanol
    DB03247 Riboflavin Monophosphate

    Proteomic databases

    EPDiP0AFI7
    PaxDbiP0AFI7
    PRIDEiP0AFI7

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74710; AAC74710; b1638
    BAA15399; BAA15399; BAA15399
    GeneIDi946806
    KEGGiecj:JW1630
    eco:b1638
    PATRICifig|1411691.4.peg.622

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB1450
    EcoGeneiEG11487 pdxH

    Phylogenomic databases

    eggNOGiENOG4108S7T Bacteria
    COG0259 LUCA
    HOGENOMiHOG000242755
    InParanoidiP0AFI7
    KOiK00275
    PhylomeDBiP0AFI7

    Enzyme and pathway databases

    UniPathwayi
    UPA01068;UER00304

    UPA01068;UER00305

    BioCyciEcoCyc:PDXH-MONOMER
    MetaCyc:PDXH-MONOMER
    BRENDAi1.4.3.5 2026

    Miscellaneous databases

    EvolutionaryTraceiP0AFI7

    Protein Ontology

    More...
    PROi
    PR:P0AFI7

    Family and domain databases

    Gene3Di2.30.110.10, 1 hit
    HAMAPiMF_01629 PdxH, 1 hit
    InterProiView protein in InterPro
    IPR000659 Pyridox_Oxase
    IPR019740 Pyridox_Oxase_CS
    IPR011576 Pyridox_Oxase_put
    IPR019576 Pyridoxamine_oxidase_dimer_C
    IPR012349 Split_barrel_FMN-bd
    PANTHERiPTHR10851 PTHR10851, 1 hit
    PfamiView protein in Pfam
    PF10590 PNP_phzG_C, 1 hit
    PF01243 Putative_PNPOx, 1 hit
    PIRSFiPIRSF000190 Pyd_amn-ph_oxd, 1 hit
    TIGRFAMsiTIGR00558 pdxH, 1 hit
    PROSITEiView protein in PROSITE
    PS01064 PYRIDOX_OXIDASE, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPDXH_ECOLI
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0AFI7
    Secondary accession number(s): P28225
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: January 23, 2007
    Last modified: December 5, 2018
    This is version 114 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again