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Entry version 179 (29 Sep 2021)
Sequence version 3 (23 Jan 2007)
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Protein

Xanthine dehydrogenase/oxidase

Gene

Xdh

Organism
Rattus norvegicus (Rat)
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.

1 Publication

<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.2 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 11
Metal bindingi48Iron-sulfur 11
Metal bindingi51Iron-sulfur 11
Metal bindingi73Iron-sulfur 11
Metal bindingi112Iron-sulfur 21
Metal bindingi115Iron-sulfur 21
Metal bindingi147Iron-sulfur 21
Metal bindingi149Iron-sulfur 21
<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 sitei336FADBy similarity1
Binding sitei359FAD2 Publications1
Binding sitei403FAD; via amide nitrogen and carbonyl oxygen2 Publications1
Binding sitei421FADBy similarity1
Metal bindingi767Molybdenum (Mo-molybdopterin metal ligand)By similarity1
Metal bindingi798Molybdenum (Mo-molybdopterin metal ligand); via carbonyl oxygenBy similarity1
Binding sitei802Substrate1
Binding sitei880Substrate1
Metal bindingi912Molybdenum (Mo-molybdopterin metal ligand); via amide nitrogenBy similarity1
Binding sitei914SubstrateBy similarity1
Binding sitei1010Substrate; via amide nitrogen1
Metal bindingi1079Molybdenum (Mo-molybdopterin metal ligand); via amide nitrogenBy similarity1
<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

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 bindingi256 – 263FAD2 Publications8
Nucleotide bindingi346 – 350FAD2 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

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-15163

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.17.1.4, 5301
1.17.3.2, 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-74259, Purine catabolism
R-RNO-8851680, Butyrophilin (BTN) family interactions

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P22985

<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:1.17.1.42 Publications)
Short name:
XD
Xanthine oxidase (EC:1.17.3.22 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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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

Organism-specific databases

Rat genome database

More...
RGDi
62043, Xdh

<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>Mutagenesisi335 – 336WF → AL: Converts the enzyme to the oxidase form that utilizes molecular oxygen as electron acceptor. Interferes with normal conversion to the dehydrogenase form by reducing agents. 1 Publication2
Mutagenesisi535C → A: Slows the conversion from the dehydrogenase form to the oxidase form; when associated with R-992. Abolishes conversion from the dehydrogenase form to the oxidase form; when associated with R-992 and S-1316. 1 Publication1
Mutagenesisi992C → R: Slows the conversion from the dehydrogenase form to the oxidase form; when associated with A-535. Abolishes conversion from the dehydrogenase form to the oxidase form; when associated with A-535 and S-1316. 1 Publication1
Mutagenesisi1316C → S: Abolishes conversion from the dehydrogenase form to the oxidase form; when associated with A-535 and R-992. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1075246

DrugCentral

More...
DrugCentrali
P22985

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001660861 – 1331Xanthine 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 form1 Publication

<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
P22985

PRoteomics IDEntifications database

More...
PRIDEi
P22985

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P22985

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P22985

<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 reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By interferon.

<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

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000009634

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P22985

<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

11331
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
P22985

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
P22985

<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
Domaini228 – 413FAD-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
P22985

Database of Orthologous Groups

More...
OrthoDBi
48717at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P22985

Family and domain databases

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>Sequence (1+)i

<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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P22985-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTADELVFFV NGKKVVEKNA DPETTLLVYL RRKLGLCGTK LGCGEGGCGA
60 70 80 90 100
CTVMISKYDR LQNKIVHFSV NACLAPICSL HHVAVTTVEG IGNTQKLHPV
110 120 130 140 150
QERIARSHGS QCGFCTPGIV MSMYTLLRNQ PEPTVEEIEN AFQGNLCRCT
160 170 180 190 200
GYRPILQGFR TFAKDGGCCG GSGNNPNCCM NQTKDQTVSL SPSLFNPEDF
210 220 230 240 250
KPLDPTQEPI FPPELLRLKD TPQKKLRFEG ERVTWIQAST MEELLDLKAQ
260 270 280 290 300
HPDAKLVVGN TEIGIEMKFK NMLFPLIVCP AWIPELNSVV HGPEGISFGA
310 320 330 340 350
SCPLSLVESV LAEEIAKLPE QKTEVFRGVM EQLRWFAGKQ VKSVASIGGN
360 370 380 390 400
IITASPISDL NPVFMASGAK LTLVSRGTRR TVRMDHTFFP GYRKTLLRPE
410 420 430 440 450
EILLSIEIPY SKEGEFFSAF KQASRREDDI AKVTSGMRVL FKPGTIEVQE
460 470 480 490 500
LSLCFGGMAD RTISALKTTP KQLSKSWNEE LLQSVCAGLA EELQLAPDAP
510 520 530 540 550
GGMVEFRRTL TLSFFFKFYL TVLQKLGRAD LEDMCGKLDP TFASATLLFQ
560 570 580 590 600
KDPPANVQLF QEVPKDQSEE DMVGRPLPHL AANMQASGEA VYCDDIPRYE
610 620 630 640 650
NELSLRLVTS TRAHAKITSI DTSEAKKVPG FVCFLTAEDV PNSNATGLFN
660 670 680 690 700
DETVFAKDEV TCVGHIIGAV VADTPEHAQR AARGVKITYE DLPAIITIQD
710 720 730 740 750
AINNNSFYGS EIKIEKGDLK KGFSEADNVV SGELYIGGQE HFYLETNCTI
760 770 780 790 800
AVPKGEAGEM ELFVSTQNTM KTQSFVAKML GVPDNRIVVR VKRMGGGFGG
810 820 830 840 850
KETRSTVVST ALALAAHKTG RPVRCMLDRD EDMLITGGRH PFLAKYKVGF
860 870 880 890 900
MKTGTVVALE VAHFSNGGNT EDLSRSIMER ALFHMDNAYK IPNIRGTGRI
910 920 930 940 950
CKTNLPSNTA FRGFGGPQGM LIAEYWMSEV AITCGLPAEE VRRKNMYKEG
960 970 980 990 1000
DLTHFNQKLE GFTLPRCWDE CIASSQYLAR KREVEKFNRE NCWKKRGLCI
1010 1020 1030 1040 1050
IPTKFGISFT LPFLNQGGAL VHVYTDGSVL LTHGGTEMGQ GLHTKMVQVA
1060 1070 1080 1090 1100
SRALKIPTSK IHISETSTNT VPNTSPTAAS ASADLNGQGV YEACQTILKR
1110 1120 1130 1140 1150
LEPFKKKKPT GPWEAWVMDA YTSAVSLSAT GFYKTPNLGY SFETNSGNPF
1160 1170 1180 1190 1200
HYFSYGVACS EVEIDCLTGD HKNLRTDIVM DVGSSLNPAI DIGQVEGAFV
1210 1220 1230 1240 1250
QGLGLFTMEE LHYSPEGSLH TRGPSTYKIP AFGSIPIEFR VSLLRDCPNK
1260 1270 1280 1290 1300
RAIYASKAVG EPPLFLASSI FFAIKDAIRA ARAQHGDNAK QLFQLDSPAT
1310 1320 1330
PEKIRNACVD QFTTLCVTGV PENCKSWSVR I
Length:1,331
Mass (Da):146,243
Last modified:January 23, 2007 - v3
<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:iBF2586A9C63A0B2C
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1LQS6F1LQS6_RAT
Xanthine dehydrogenase
Xdh rCG_61833
1,331Annotation 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>

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
J05579 mRNA Translation: AAA42349.1
AH000836 Unassigned DNA Translation: AAA18869.1

NCBI Reference Sequences

More...
RefSeqi
NP_058850.1, NM_017154.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
497811

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:497811

UCSC genome browser

More...
UCSCi
RGD:62043, rat

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05579 mRNA Translation: AAA42349.1
AH000836 Unassigned DNA Translation: AAA18869.1
RefSeqiNP_058850.1, NM_017154.1

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
1WYGX-ray2.60A1-1331[»]
2E3TX-ray2.28A/B1-1331[»]
3AN1X-ray1.73A/B1-1331[»]
4YRWX-ray1.99A/B1-1315[»]
4YSWX-ray1.99A/B1-1315[»]
4YTYX-ray2.20A/B1-1331[»]
4YTZX-ray2.30A/B1-1315[»]
6A7XX-ray2.15A/B1-1331[»]
6ABUX-ray1.77A/B1-1331[»]
6AC1X-ray1.77A/B1-1331[»]
6AC4X-ray2.19A/B1-1331[»]
6AD4X-ray1.80A/B1-1331[»]
6ADJX-ray2.18A/B1-1331[»]
6AJUX-ray1.94A/F1-1331[»]
SMRiP22985
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009634

Chemistry databases

BindingDBiP22985
ChEMBLiCHEMBL1075246
DrugCentraliP22985

PTM databases

iPTMnetiP22985
PhosphoSitePlusiP22985

Proteomic databases

PaxDbiP22985
PRIDEiP22985

Genome annotation databases

GeneIDi497811
KEGGirno:497811
UCSCiRGD:62043, rat

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
7498
RGDi62043, Xdh

Phylogenomic databases

eggNOGiKOG0430, Eukaryota
InParanoidiP22985
OrthoDBi48717at2759
PhylomeDBiP22985

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15163
BRENDAi1.17.1.4, 5301
1.17.3.2, 5301
ReactomeiR-RNO-74259, Purine catabolism
R-RNO-8851680, Butyrophilin (BTN) family interactions
SABIO-RKiP22985

Miscellaneous databases

EvolutionaryTraceiP22985

Protein Ontology

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PROi
PR:P22985

Family and domain databases

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_RAT
<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: P22985
Secondary accession number(s): Q63157
<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: August 1, 1991
Last sequence update: January 23, 2007
Last modified: September 29, 2021
This is version 179 of the entry and version 3 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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