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Entry version 173 (29 Sep 2021)
Sequence version 4 (23 Jan 2007)
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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 <a href="http://www.uniprot.org/help/function_section">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_section">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_section">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 bindingi767Molybdenum (Mo-molybdopterin metal ligand)3 Publications1
Metal bindingi798Molybdenum (Mo-molybdopterin metal ligand); via carbonyl oxygen3 Publications1
Binding sitei802Substrate1
Binding sitei880Substrate1
Metal bindingi912Molybdenum (Mo-molybdopterin metal ligand); via amide nitrogen3 Publications1
Binding sitei914Substrate1
Binding sitei1010Substrate; via amide nitrogen1
Metal bindingi1079Molybdenum (Mo-molybdopterin metal ligand); via amide nitrogen3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_section">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

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaRuminantiaPecoraBovidaeBovinaeBos
<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

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

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_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 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_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

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

More...
SMRi
P80457

Database of comparative protein structure models

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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_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

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

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.10.20.30, 1 hit
3.30.43.10, 1 hit
3.30.465.10, 1 hit

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
IPR012675, Beta-grasp_dom_sf
IPR005107, CO_DH_flav_C
IPR036683, CO_DH_flav_C_dom_sf
IPR016166, FAD-bd_PCMH
IPR036318, FAD-bd_PCMH-like_sf
IPR016167, FAD-bd_PCMH_sub1
IPR016169, FAD-bd_PCMH_sub2
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>. 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_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

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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

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PIRi
S65135

NCBI Reference Sequences

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RefSeqi
NP_776397.1, NM_173972.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
280960

KEGG: Kyoto Encyclopedia of Genes and Genomes

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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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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

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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

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PROi
PR:P80457

Family and domain databases

DisProtiDP00450
Gene3Di3.10.20.30, 1 hit
3.30.43.10, 1 hit
3.30.465.10, 1 hit
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
IPR012675, Beta-grasp_dom_sf
IPR005107, CO_DH_flav_C
IPR036683, CO_DH_flav_C_dom_sf
IPR016166, FAD-bd_PCMH
IPR036318, FAD-bd_PCMH-like_sf
IPR016167, FAD-bd_PCMH_sub1
IPR016169, FAD-bd_PCMH_sub2
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

MobiDB: a database of protein disorder and mobility annotations

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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_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: September 29, 2021
This is version 173 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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