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Protein

Xanthine dehydrogenase/oxidase

Gene

XDH

Organism
Bos taurus (Bovine)
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

Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species.By similarity

<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

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Can be converted from the dehydrogenase form (D) to the oxidase form (O) irreversibly by proteolysis or reversibly through the oxidation of sulfhydryl groups.3 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

  1. KM=111 µM for molecular oxygen in dehydrogenase form2 Publications
  2. KM=37.7 µM for molecular oxygen in oxygenase form2 Publications
  3. KM=20.8 µM for NAD2 Publications
  4. KM=5 µM for xanthine2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi43Iron-sulfur 13 Publications1
    Metal bindingi48Iron-sulfur 13 Publications1
    Metal bindingi51Iron-sulfur 13 Publications1
    Metal bindingi73Iron-sulfur 13 Publications1
    Metal bindingi113Iron-sulfur 23 Publications1
    Metal bindingi116Iron-sulfur 23 Publications1
    Metal bindingi148Iron-sulfur 23 Publications1
    Metal bindingi150Iron-sulfur 23 Publications1
    <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 sitei337FAD2 Publications1
    Binding sitei360FAD2 Publications1
    Binding sitei404FAD; via amide nitrogen and carbonyl oxygen2 Publications1
    Binding sitei422FAD2 Publications1
    Metal bindingi767Molybdenum3 Publications1
    Metal bindingi798Molybdenum; via carbonyl oxygen3 Publications1
    Binding sitei802Substrate1
    Binding sitei880Substrate1
    Metal bindingi912Molybdenum; via amide nitrogen3 Publications1
    Binding sitei914Substrate1
    Binding sitei1010Substrate; via amide nitrogen1
    Metal bindingi1079Molybdenum; via amide nitrogen3 Publications1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1261Proton acceptor1 Publication1

    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 bindingi257 – 264FAD2 Publications8
    Nucleotide bindingi347 – 351FAD2 Publications5

    <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
    Ligand2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.17.1.4 908
    1.17.3.2 908

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P80457

    <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:
    Xanthine dehydrogenase/oxidase
    Including the following 2 domains:
    Xanthine dehydrogenase (EC:1.17.1.44 Publications)
    Short name:
    XD
    Xanthine oxidase (EC:1.17.3.24 Publications)
    Short name:
    XO
    Alternative name(s):
    Xanthine oxidoreductase
    Short name:
    XOR
    <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:XDH
    <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>OrganismiBos taurus (Bovine)
    <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 identifieri9913 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    <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
    • UP000009136 <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: Unplaced

    <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

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, Peroxisome, Secreted

    <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>Mutagenesisi335R → A: Promotes conversion to the oxidase form that utilizes molecular oxygen as electron acceptor. Interferes with normal conversion to the dehydrogenase form by reducing agents. 1 Publication1
    Mutagenesisi336W → A: Promotes conversion to the oxidase form that utilizes molecular oxygen as electron acceptor. Interferes with normal conversion to the dehydrogenase form by reducing agents. 1 Publication1
    Mutagenesisi427R → Q: Promotes conversion to the oxidase form that utilizes molecular oxygen as electron acceptor. Interferes with normal conversion to the dehydrogenase form by reducing agents. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3649

    <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_00001660822 – 1332Xanthine dehydrogenase/oxidaseAdd BLAST1331

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi535 ↔ 992In oxidase formBy similarity

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Subject to partial proteolysis; this alters the enzyme from the dehydrogenase form (D) to the oxidase form (O).
    Contains sulfhydryl groups that are easily oxidized (in vitro); this alters the enzyme from the dehydrogenase form (D) to the oxidase form (O).

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

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

    More...
    PaxDbi
    P80457

    PeptideAtlas

    More...
    PeptideAtlasi
    P80457

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P80457

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Detected in milk (at protein level).3 Publications

    <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. Interacts with BTN1A1 (By similarity).By similarity

    GO - Molecular functioni

    Protein-protein interaction databases

    Protein interaction database and analysis system

    More...
    IntActi
    P80457, 1 interactor

    STRING: functional protein association networks

    More...
    STRINGi
    9913.ENSBTAP00000016620

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P80457

    <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

    11332
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    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
    1FIQX-ray2.50A1-219[»]
    B220-569[»]
    C570-1332[»]
    1FO4X-ray2.10A/B1-1332[»]
    1N5XX-ray2.80A/B2-1332[»]
    1V97X-ray1.94A/B1-1332[»]
    1VDVX-ray1.98A/B1-1332[»]
    3AM9X-ray2.17A/B1-1332[»]
    3AMZX-ray2.10A/B1-1332[»]
    3AX7X-ray2.34A/B1-1332[»]
    3AX9X-ray2.30A/B1-1332[»]
    3B9JX-ray2.30A/I1-219[»]
    B/J220-569[»]
    C/K570-1332[»]
    3BDJX-ray2.00A/B1-1332[»]
    3ETRX-ray2.20A/L2-165[»]
    B/M224-528[»]
    C/N571-1325[»]
    3EUBX-ray2.602/A/J/S1-165[»]
    3/B/K/T224-528[»]
    4/C/L/U571-1332[»]
    3NRZX-ray1.80A/J2-165[»]
    B/K224-528[»]
    C/L571-1326[»]
    3NS1X-ray2.60A/J2-165[»]
    B/K224-528[»]
    C/L571-1325[»]
    3NVVX-ray1.82A/J2-165[»]
    B/K195-528[»]
    C/L571-1325[»]
    3NVWX-ray1.60A/J2-165[»]
    B/K195-528[»]
    C/L571-1326[»]
    3NVYX-ray2.00A/J2-165[»]
    B/K195-528[»]
    C/L571-1326[»]
    3NVZX-ray1.60A/J2-165[»]
    B/K224-528[»]
    C/L571-1325[»]
    3SR6X-ray2.10A/J2-165[»]
    B/K224-528[»]
    C/L571-1315[»]
    3UNAX-ray1.90A/B1-1332[»]
    3UNCX-ray1.65A/B1-1332[»]
    3UNIX-ray2.20A/B1-1332[»]

    Database of protein disorder

    More...
    DisProti
    DP00450

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P80457

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

    More...
    SMRi
    P80457

    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
    P80457

    <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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini4 – 912Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST88
    Domaini229 – 414FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST186

    <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 xanthine dehydrogenase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0430 Eukaryota
    COG4630 LUCA
    COG4631 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000191197

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG004182

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P80457

    KEGG Orthology (KO)

    More...
    KOi
    K00106

    Database of Orthologous Groups

    More...
    OrthoDBi
    48717at2759

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR002888 2Fe-2S-bd
    IPR036884 2Fe-2S-bd_dom_sf
    IPR036010 2Fe-2S_ferredoxin-like_sf
    IPR001041 2Fe-2S_ferredoxin-type
    IPR006058 2Fe2S_fd_BS
    IPR000674 Ald_Oxase/Xan_DH_a/b
    IPR036856 Ald_Oxase/Xan_DH_a/b_sf
    IPR016208 Ald_Oxase/xanthine_DH
    IPR008274 AldOxase/xan_DH_Mopterin-bd
    IPR037165 AldOxase/xan_DH_Mopterin-bd_sf
    IPR005107 CO_DH_flav_C
    IPR036683 CO_DH_flav_C_dom_sf
    IPR016166 FAD-bd_PCMH
    IPR036318 FAD-bd_PCMH-like_sf
    IPR002346 Mopterin_DH_FAD-bd
    IPR022407 OxRdtase_Mopterin_BS
    IPR014307 Xanthine_DH_ssu

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01315 Ald_Xan_dh_C, 1 hit
    PF02738 Ald_Xan_dh_C2, 1 hit
    PF03450 CO_deh_flav_C, 1 hit
    PF00941 FAD_binding_5, 1 hit
    PF00111 Fer2, 1 hit
    PF01799 Fer2_2, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000127 Xanthine_DH, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM01008 Ald_Xan_dh_C, 1 hit
    SM01092 CO_deh_flav_C, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF47741 SSF47741, 1 hit
    SSF54292 SSF54292, 1 hit
    SSF54665 SSF54665, 1 hit
    SSF55447 SSF55447, 1 hit
    SSF56003 SSF56003, 1 hit
    SSF56176 SSF56176, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR02963 xanthine_xdhA, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00197 2FE2S_FER_1, 1 hit
    PS51085 2FE2S_FER_2, 1 hit
    PS51387 FAD_PCMH, 1 hit
    PS00559 MOLYBDOPTERIN_EUK, 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.

    P80457-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTADELVFFV NGKKVVEKNA DPETTLLAYL RRKLGLRGTK LGCGEGGCGA
    60 70 80 90 100
    CTVMLSKYDR LQDKIIHFSA NACLAPICTL HHVAVTTVEG IGSTKTRLHP
    110 120 130 140 150
    VQERIAKSHG SQCGFCTPGI VMSMYTLLRN QPEPTVEEIE DAFQGNLCRC
    160 170 180 190 200
    TGYRPILQGF RTFAKNGGCC GGNGNNPNCC MNQKKDHTVT LSPSLFNPEE
    210 220 230 240 250
    FMPLDPTQEP IFPPELLRLK DVPPKQLRFE GERVTWIQAS TLKELLDLKA
    260 270 280 290 300
    QHPEAKLVVG NTEIGIEMKF KNQLFPMIIC PAWIPELNAV EHGPEGISFG
    310 320 330 340 350
    AACALSSVEK TLLEAVAKLP TQKTEVFRGV LEQLRWFAGK QVKSVASLGG
    360 370 380 390 400
    NIITASPISD LNPVFMASGT KLTIVSRGTR RTVPMDHTFF PSYRKTLLGP
    410 420 430 440 450
    EEILLSIEIP YSREDEFFSA FKQASRREDD IAKVTCGMRV LFQPGSMQVK
    460 470 480 490 500
    ELALCYGGMA DRTISALKTT QKQLSKFWNE KLLQDVCAGL AEELSLSPDA
    510 520 530 540 550
    PGGMIEFRRT LTLSFFFKFY LTVLKKLGKD SKDKCGKLDP TYTSATLLFQ
    560 570 580 590 600
    KDPPANIQLF QEVPNGQSKE DTVGRPLPHL AAAMQASGEA VYCDDIPRYE
    610 620 630 640 650
    NELFLRLVTS TRAHAKIKSI DVSEAQKVPG FVCFLSADDI PGSNETGLFN
    660 670 680 690 700
    DETVFAKDTV TCVGHIIGAV VADTPEHAER AAHVVKVTYE DLPAIITIED
    710 720 730 740 750
    AIKNNSFYGS ELKIEKGDLK KGFSEADNVV SGELYIGGQD HFYLETHCTI
    760 770 780 790 800
    AIPKGEEGEM ELFVSTQNAM KTQSFVAKML GVPVNRILVR VKRMGGGFGG
    810 820 830 840 850
    KETRSTLVSV AVALAAYKTG HPVRCMLDRN EDMLITGGRH PFLARYKVGF
    860 870 880 890 900
    MKTGTIVALE VDHYSNAGNS RDLSHSIMER ALFHMDNCYK IPNIRGTGRL
    910 920 930 940 950
    CKTNLSSNTA FRGFGGPQAL FIAENWMSEV AVTCGLPAEE VRWKNMYKEG
    960 970 980 990 1000
    DLTHFNQRLE GFSVPRCWDE CLKSSQYYAR KSEVDKFNKE NCWKKRGLCI
    1010 1020 1030 1040 1050
    IPTKFGISFT VPFLNQAGAL IHVYTDGSVL VSHGGTEMGQ GLHTKMVQVA
    1060 1070 1080 1090 1100
    SKALKIPISK IYISETSTNT VPNSSPTAAS VSTDIYGQAV YEACQTILKR
    1110 1120 1130 1140 1150
    LEPFKKKNPD GSWEDWVMAA YQDRVSLSTT GFYRTPNLGY SFETNSGNAF
    1160 1170 1180 1190 1200
    HYFTYGVACS EVEIDCLTGD HKNLRTDIVM DVGSSLNPAI DIGQVEGAFV
    1210 1220 1230 1240 1250
    QGLGLFTLEE LHYSPEGSLH TRGPSTYKIP AFGSIPTEFR VSLLRDCPNK
    1260 1270 1280 1290 1300
    KAIYASKAVG EPPLFLGASV FFAIKDAIRA ARAQHTNNNT KELFRLDSPA
    1310 1320 1330
    TPEKIRNACV DKFTTLCVTG APGNCKPWSL RV
    Length:1,332
    Mass (Da):146,790
    Last modified:January 23, 2007 - v4
    <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:i744BA523471948B7
    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 conflicti188T → TQ in CAA67117 (PubMed:9388547).Curated1
    Sequence conflicti199E → K in CAA67117 (PubMed:9388547).Curated1
    Sequence conflicti366M → V in CAA67117 (PubMed:9388547).Curated1
    Sequence conflicti552D → H in CAA58497 (PubMed:8708081).Curated1
    Sequence conflicti958R → K in CAA67117 (PubMed:9388547).Curated1
    Sequence conflicti976Q → E in CAA67117 (PubMed:9388547).Curated1
    Sequence conflicti1039 – 1040GQ → E in CAA67117 (PubMed:9388547).Curated2
    Sequence conflicti1244L → V in CAA67117 (PubMed:9388547).Curated1
    Sequence conflicti1268A → P in CAA67117 (PubMed:9388547).Curated1
    Sequence conflicti1279 – 1281RAA → ARG in CAA67117 (PubMed:9388547).Curated3

    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
    X83508 mRNA Translation: CAA58497.1
    X98491 mRNA Translation: CAA67117.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S65135

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_776397.1, NM_173972.2

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Bt.5403

    Genome annotation databases

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    280960

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    bta:280960

    <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

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    Worthington enzyme manual

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X83508 mRNA Translation: CAA58497.1
    X98491 mRNA Translation: CAA67117.1
    PIRiS65135
    RefSeqiNP_776397.1, NM_173972.2
    UniGeneiBt.5403

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1FIQX-ray2.50A1-219[»]
    B220-569[»]
    C570-1332[»]
    1FO4X-ray2.10A/B1-1332[»]
    1N5XX-ray2.80A/B2-1332[»]
    1V97X-ray1.94A/B1-1332[»]
    1VDVX-ray1.98A/B1-1332[»]
    3AM9X-ray2.17A/B1-1332[»]
    3AMZX-ray2.10A/B1-1332[»]
    3AX7X-ray2.34A/B1-1332[»]
    3AX9X-ray2.30A/B1-1332[»]
    3B9JX-ray2.30A/I1-219[»]
    B/J220-569[»]
    C/K570-1332[»]
    3BDJX-ray2.00A/B1-1332[»]
    3ETRX-ray2.20A/L2-165[»]
    B/M224-528[»]
    C/N571-1325[»]
    3EUBX-ray2.602/A/J/S1-165[»]
    3/B/K/T224-528[»]
    4/C/L/U571-1332[»]
    3NRZX-ray1.80A/J2-165[»]
    B/K224-528[»]
    C/L571-1326[»]
    3NS1X-ray2.60A/J2-165[»]
    B/K224-528[»]
    C/L571-1325[»]
    3NVVX-ray1.82A/J2-165[»]
    B/K195-528[»]
    C/L571-1325[»]
    3NVWX-ray1.60A/J2-165[»]
    B/K195-528[»]
    C/L571-1326[»]
    3NVYX-ray2.00A/J2-165[»]
    B/K195-528[»]
    C/L571-1326[»]
    3NVZX-ray1.60A/J2-165[»]
    B/K224-528[»]
    C/L571-1325[»]
    3SR6X-ray2.10A/J2-165[»]
    B/K224-528[»]
    C/L571-1315[»]
    3UNAX-ray1.90A/B1-1332[»]
    3UNCX-ray1.65A/B1-1332[»]
    3UNIX-ray2.20A/B1-1332[»]
    DisProtiDP00450
    ProteinModelPortaliP80457
    SMRiP80457
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP80457, 1 interactor
    STRINGi9913.ENSBTAP00000016620

    Chemistry databases

    BindingDBiP80457
    ChEMBLiCHEMBL3649

    Proteomic databases

    PaxDbiP80457
    PeptideAtlasiP80457
    PRIDEiP80457

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi280960
    KEGGibta:280960

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    7498

    Phylogenomic databases

    eggNOGiKOG0430 Eukaryota
    COG4630 LUCA
    COG4631 LUCA
    HOGENOMiHOG000191197
    HOVERGENiHBG004182
    InParanoidiP80457
    KOiK00106
    OrthoDBi48717at2759

    Enzyme and pathway databases

    BRENDAi1.17.1.4 908
    1.17.3.2 908
    SABIO-RKiP80457

    Miscellaneous databases

    EvolutionaryTraceiP80457

    Protein Ontology

    More...
    PROi
    PR:P80457

    Family and domain databases

    InterProiView protein in InterPro
    IPR002888 2Fe-2S-bd
    IPR036884 2Fe-2S-bd_dom_sf
    IPR036010 2Fe-2S_ferredoxin-like_sf
    IPR001041 2Fe-2S_ferredoxin-type
    IPR006058 2Fe2S_fd_BS
    IPR000674 Ald_Oxase/Xan_DH_a/b
    IPR036856 Ald_Oxase/Xan_DH_a/b_sf
    IPR016208 Ald_Oxase/xanthine_DH
    IPR008274 AldOxase/xan_DH_Mopterin-bd
    IPR037165 AldOxase/xan_DH_Mopterin-bd_sf
    IPR005107 CO_DH_flav_C
    IPR036683 CO_DH_flav_C_dom_sf
    IPR016166 FAD-bd_PCMH
    IPR036318 FAD-bd_PCMH-like_sf
    IPR002346 Mopterin_DH_FAD-bd
    IPR022407 OxRdtase_Mopterin_BS
    IPR014307 Xanthine_DH_ssu
    PfamiView protein in Pfam
    PF01315 Ald_Xan_dh_C, 1 hit
    PF02738 Ald_Xan_dh_C2, 1 hit
    PF03450 CO_deh_flav_C, 1 hit
    PF00941 FAD_binding_5, 1 hit
    PF00111 Fer2, 1 hit
    PF01799 Fer2_2, 1 hit
    PIRSFiPIRSF000127 Xanthine_DH, 1 hit
    SMARTiView protein in SMART
    SM01008 Ald_Xan_dh_C, 1 hit
    SM01092 CO_deh_flav_C, 1 hit
    SUPFAMiSSF47741 SSF47741, 1 hit
    SSF54292 SSF54292, 1 hit
    SSF54665 SSF54665, 1 hit
    SSF55447 SSF55447, 1 hit
    SSF56003 SSF56003, 1 hit
    SSF56176 SSF56176, 1 hit
    TIGRFAMsiTIGR02963 xanthine_xdhA, 1 hit
    PROSITEiView protein in PROSITE
    PS00197 2FE2S_FER_1, 1 hit
    PS51085 2FE2S_FER_2, 1 hit
    PS51387 FAD_PCMH, 1 hit
    PS00559 MOLYBDOPTERIN_EUK, 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 nameiXDH_BOVIN
    <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: P80457
    Secondary accession number(s): Q95325
    <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: February 1, 1996
    Last sequence update: January 23, 2007
    Last modified: January 16, 2019
    This is version 163 of the entry and version 4 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 programChordata 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. SIMILARITY comments
      Index of protein domains and families
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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