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UniProtKB - P80457 (XDH_BOVIN)

Entry version 171 (07 Apr 2021)
Sequence version 4 (23 Jan 2007)
Previous versions | rss
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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%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

    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%5Fand%5Fbiotech%5Fsection">'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

    DrugCentral

    More...    DrugCentrali    		P80457

    <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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<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%5Fprocessing%5Fsection">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%5Fsection">'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%5Fsection">'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

    Complete GO annotation on QuickGO ...

    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

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

    More...    SMRi    		P80457

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		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%5Fand%5Fdomains%5Fsection">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

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P80457

    Database of Orthologous Groups

    More...    OrthoDBi    		48717at2759

    Family and domain databases

    Database of protein disorder

    More...    DisProti    		DP00450

    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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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

    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%5Freferences%5Fsection">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

    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[»]
    SMRiP80457
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    IntActiP80457, 1 interactor
    STRINGi9913.ENSBTAP00000016620

    Chemistry databases

    BindingDBiP80457
    ChEMBLiCHEMBL3649
    DrugCentraliP80457

    Proteomic databases

    PaxDbiP80457
    PeptideAtlasiP80457
    PRIDEiP80457

    Genome annotation databases

    GeneIDi280960
    KEGGibta:280960

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		7498

    Phylogenomic databases

    eggNOGiKOG0430, Eukaryota
    InParanoidiP80457
    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

    DisProtiDP00450
    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...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		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%5Fand%5Fisoforms">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: April 7, 2021
    This is version 171 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, 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
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