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Protein

p-hydroxybenzoate hydroxylase

Gene

pobA

Organism
Pseudomonas fluorescens
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 incorporation of an atom of dioxygen into p-hydroxybenzoate (p-OHB) to form 3,4-dihydroxybenzoate (3,4DOHB). The reaction occurs in two parts: reduction of the flavin adenine dinucleotide (FAD) in the enzyme by reduced nicotinamide adenine dinucleotide phosphate (NADPH) in response to binding p-hydroxybenzoate to the enzyme and oxidation of reduced FAD with oxygen to form a hydroperoxide, which then oxygenates p-hydroxybenzoate.10 Publications

<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

FAD9 PublicationsNote: Binds 1 FAD per subunit.7 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 55 sec(-1) for hydroxylase activity (PubMed:9578477, PubMed:9694855). Kcat is 55 sec(-1) for hydroxylase activity (at 25 degrees Celsius) (PubMed:1459126). Kcat is 55 sec(-1) for hydroxylase activity (at pH 8) (PubMed:10025942, PubMed:10493859). Kcat is 9 sec(-1) for hydroxylase activity (at 6 degrees Celsius) (PubMed:1459126).6 Publications
  1. KM=15 µM for p-OHB1 Publication
  2. KM=15 µM for p-OHB (at pH 6)2 Publications
  3. KM=20 µM for p-OHB2 Publications
  4. KM=25 µM for p-OHB (at 25 degrees Celsius)1 Publication
  5. KM=30 µM for NADPH1 Publication
  6. KM=30 µM for p-OHB (at 6 degrees Celsius)1 Publication
  7. KM=34 µM for NADPH (at pH 6)2 Publications
  8. KM=40 µM for NADPH (at 6 degrees Celsius)1 Publication
  9. KM=50 µM for NADPH (at 25 degrees Celsius)1 Publication
  10. KM=50 µM for NADPH1 Publication
  11. KM=70 µM for NADPH1 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: benzoate degradation via hydroxylation

    This protein is involved in step 2 of the subpathway that synthesizes 3,4-dihydroxybenzoate from benzoate.Curated
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. p-hydroxybenzoate hydroxylase (pobA)
    This subpathway is part of the pathway benzoate degradation via hydroxylation, which is itself part of Aromatic compound metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 3,4-dihydroxybenzoate from benzoate, the pathway benzoate degradation via hydroxylation and in Aromatic compound 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 sitei13FAD10 Publications1
    Binding sitei32FAD10 Publications1
    Binding sitei102FAD10 Publications1
    Binding sitei201Substrate10 Publications1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei201Important for catalytic activityBy similarity1
    Binding sitei222Substrate10 Publications1
    Binding sitei286FAD10 Publications1
    Binding sitei293Substrate; via carbonyl oxygen10 Publications1
    Sitei385Important for catalytic activityBy similarity1

    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 bindingi42 – 47FAD10 Publications6
    Nucleotide bindingi299 – 300FAD10 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 functionMonooxygenase, Oxidoreductase
    Biological processAromatic hydrocarbons catabolism
    LigandFAD, Flavoprotein, NADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-11534

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.14.13.2 5121

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

    More...
    UniPathwayi
    UPA00156;UER00257

    <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:
    p-hydroxybenzoate hydroxylase1 Publication (EC:1.14.13.27 Publications)
    Short name:
    PHBH1 Publication
    Short name:
    PHBHase1 Publication
    Alternative name(s):
    4-hydroxybenzoate 3-monooxygenaseCurated
    <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:pobA
    <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>OrganismiPseudomonas fluorescens
    <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 identifieri294 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    <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>Mutagenesisi33R → E: Slight decrease of affinity for p-OHB and strong decrease of affinity for NADPH. 1 Publication1
    Mutagenesisi33R → K: Slight decrease of affinity for p-OHB and NADPH. 1 Publication1
    Mutagenesisi33R → S: Slight decrease of affinity for p-OHB and strong decrease of affinity for NADPH. 1 Publication1
    Mutagenesisi34Q → K: Slight decrease of affinity for p-OHB and NADPH. 1 Publication1
    Mutagenesisi34Q → R: Slight decrease of affinity for p-OHB and NADPH. 1 Publication1
    Mutagenesisi34Q → T: Slight decrease of affinity for p-OHB and NADPH. 1 Publication1
    Mutagenesisi38Y → E: Slight decrease of affinity for p-OHB and strong decrease of affinity for NADPH. 1 Publication1
    Mutagenesisi38Y → F: Slight decrease of affinity for p-OHB and strong decrease of affinity for NADPH. 1 Publication1
    Mutagenesisi38Y → K: Slight decrease of affinity for p-OHB and strong decrease of affinity for NADPH. 1 Publication1
    Mutagenesisi42R → K: 4-fold and 10-fold decrease of affinity for p-OHB and NADPH, respectively. The turnover rate of p-hydroxybenzoate hydroxylase results from impaired binding of NADPH. 1 Publication1
    Mutagenesisi42R → S: 3-fold and 10-fold decrease of affinity for p-OHB and NADPH, respectively. The turnover rate of p-hydroxybenzoate hydroxylase results from impaired binding of NADPH. Hardly disturbs the binding of FAD. 1 Publication1
    Mutagenesisi44R → K: Decrease of affinity for the flavin prosthetic group. It affects NADPH binding, resulting in a low yield of the charge-transfer species between reduced flavin and NADP. 1 Publication1
    Mutagenesisi116C → S: Slight decrease of affinity for NADPH and p-OHB are observed. 1 Publication1
    Mutagenesisi161F → A: Decrease of affinity for NADPH. 1 Publication1
    Mutagenesisi161F → G: Decrease of affinity for NADPH. 1 Publication1
    Mutagenesisi162H → D: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases strongly. 1 Publication1
    Mutagenesisi162H → K: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases slightly. 1 Publication1
    Mutagenesisi162H → N: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases strongly. 1 Publication1
    Mutagenesisi162H → R: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases slightly. 1 Publication1
    Mutagenesisi162H → S: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases strongly. 1 Publication1
    Mutagenesisi162H → T: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases strongly. 1 Publication1
    Mutagenesisi162H → Y: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases slightly. 1 Publication1
    Mutagenesisi166R → E: Loses the ability to bind NADPH and FAD. 1 Publication1
    Mutagenesisi166R → K: Loses the ability to bind NADPH. 1 Publication1
    Mutagenesisi166R → S: Loses the ability to bind NADPH. 1 Publication1
    Mutagenesisi214R → K: Strong decrease of affinity for NADPH and 4-fold decrease of affinity for p-OHB are observed. 1 Publication1
    Mutagenesisi222Y → A: Results in the removal of a large side chain involving in the binding of the carboxyl group of the substrate. 1 Publication1
    Mutagenesisi269R → D: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases strongly. 1 Publication1
    Mutagenesisi269R → K: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases slightly. 1 Publication1
    Mutagenesisi269R → N: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases strongly. 1 Publication1
    Mutagenesisi269R → S: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases slightly. 1 Publication1
    Mutagenesisi269R → T: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases strongly. 1 Publication1
    Mutagenesisi269R → Y: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases strongly. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3675

    Drug and drug target database

    More...
    DrugBanki
    DB02362 4-Aminobenzoic Acid
    DB02059 Adenosine-5-Diphosphoribose
    DB03147 Flavin adenine dinucleotide
    DB04242 P-Hydroxybenzoic Acid

    <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 ‘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_00000583821 – 394p-hydroxybenzoate hydroxylaseAdd BLAST394

    <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.11 Publications

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P00438

    <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

    1394
    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
    P00438

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

    More...
    SMRi
    P00438

    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
    P00438

    <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>Regioni212 – 214Substrate binding10 Publications3

    <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

    Belongs to the aromatic-ring hydroxylase family.Curated

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.50.50.60, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR002938 FAD-bd
    IPR036188 FAD/NAD-bd_sf
    IPR012733 HB_mOase

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01494 FAD_binding_3, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51905 SSF51905, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR02360 pbenz_hydroxyl, 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.

    P00438-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKTQVAIIGA GPSGLLLGQL LHKAGIDNVI LERQTPDYVL GRIRAGVLEQ
    60 70 80 90 100
    GMVDLLREAG VDRRMARDGL VHEGVEIAFA GQRRRIDLKR LSGGKTVTVY
    110 120 130 140 150
    GQTEVTRDLM EAREACGATT VYQAAEVRLH DLQGERPYVT FERDGERLRL
    160 170 180 190 200
    DCDYIAGCDG FHGISRQSIP AERLKVFERV YPFGWLGLLA DTPPVSHELI
    210 220 230 240 250
    YANHPRGFAL CSQRSATRSR YYVQVPLTEK VEDWSDERFW TELKARLPAE
    260 270 280 290 300
    VAEKLVTGPS LEKSIAPLRS FVVEPMQHGR LFLAGDAAHI VPPTGAKGLN
    310 320 330 340 350
    LAASDVSTLY RLLLKAYREG RGELLERYSA ICLRRIWKAE RFSWWMTSVL
    360 370 380 390
    HRFPDTDAFS QRIQQTELEY YLGSEAGLAT IAENYVGLPY EEIE
    Length:394
    Mass (Da):44,322
    Last modified:April 1, 1993 - 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:iD29599224AC81E00
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti344W → Y AA sequence (PubMed:6809053).Curated1

    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
    X68438 Genomic DNA Translation: CAA48483.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A90643 WHPSBF

    <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
    X68438 Genomic DNA Translation: CAA48483.1
    PIRiA90643 WHPSBF

    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
    1BF3X-ray2.20A1-394[»]
    1BGJX-ray3.00A1-394[»]
    1BGNX-ray2.00A1-394[»]
    1BKWX-ray2.20A1-394[»]
    1CC4X-ray2.00A1-394[»]
    1CC6X-ray2.20A1-394[»]
    1CJ2X-ray2.80A1-391[»]
    1CJ3X-ray2.50A1-392[»]
    1CJ4X-ray2.40A1-392[»]
    1PBBX-ray2.50A1-394[»]
    1PBCX-ray2.80A1-394[»]
    1PBDX-ray2.30A1-394[»]
    1PBEX-ray1.90A1-394[»]
    1PBFX-ray2.70A1-394[»]
    1PDHX-ray2.10A1-394[»]
    1PHHX-ray2.30A1-394[»]
    2PHHX-ray2.70A1-394[»]
    ProteinModelPortaliP00438
    SMRiP00438
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry databases

    BindingDBiP00438
    ChEMBLiCHEMBL3675
    DrugBankiDB02362 4-Aminobenzoic Acid
    DB02059 Adenosine-5-Diphosphoribose
    DB03147 Flavin adenine dinucleotide
    DB04242 P-Hydroxybenzoic Acid

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayi
    UPA00156;UER00257

    BioCyciMetaCyc:MONOMER-11534
    BRENDAi1.14.13.2 5121

    Miscellaneous databases

    EvolutionaryTraceiP00438

    Family and domain databases

    Gene3Di3.50.50.60, 1 hit
    InterProiView protein in InterPro
    IPR002938 FAD-bd
    IPR036188 FAD/NAD-bd_sf
    IPR012733 HB_mOase
    PfamiView protein in Pfam
    PF01494 FAD_binding_3, 1 hit
    SUPFAMiSSF51905 SSF51905, 1 hit
    TIGRFAMsiTIGR02360 pbenz_hydroxyl, 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 nameiPHHY_PSEFL
    <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: P00438
    <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: July 21, 1986
    Last sequence update: April 1, 1993
    Last modified: December 5, 2018
    This is version 118 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, Direct protein sequencing

    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
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