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P47989 (XDH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Xanthine dehydrogenase/oxidase

Including the following 2 domains:

  1. Xanthine dehydrogenase
    Short name=XD
    EC=1.17.1.4
  2. Xanthine oxidase
    Short name=XO
    EC=1.17.3.2
    Alternative name(s):
    Xanthine oxidoreductase
    Short name=XOR
Gene names
Name:XDH
Synonyms:XDHA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Has also low oxidase activity towards aldehydes (in vitro). Ref.10

Catalytic activity

Hypoxanthine + NAD+ + H2O = xanthine + NADH. Ref.5 Ref.10

Xanthine + H2O + O2 = urate + H2O2. Ref.5 Ref.10

Cofactor

Binds 2 2Fe-2S clusters. Ref.10

FAD. Ref.10

Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per subunit. Ref.10

Enzyme regulation

Can be converted from the dehydrogenase form (D) to the oxidase form (O) irreversibly by proteolysis or reversibly through the oxidation of sulfhydryl groups By similarity. Ref.11

Subunit structure

Homodimer. Interacts with BTN1A1 By similarity. Ref.10

Subcellular location

Cytoplasm By similarity. Peroxisome By similarity. Secreted.

Tissue specificity

Detected in milk (at protein level). Ref.11

Post-translational modification

Subject to partial proteolysis; this alters the enzyme from the dehydrogenase form (D) to the oxidase form (O) By similarity.

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

Involvement in disease

Xanthinuria 1 (XU1) [MIM:278300]: A disorder characterized by excretion of very large amounts of xanthine in the urine and a tendency to form xanthine stones. Uric acid is strikingly diminished in serum and urine. Xanthinuria 1 is due to isolated xanthine dehydrogenase deficiency. Patients can metabolize allopurinol.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.8 Ref.12 Ref.13

Sequence similarities

Belongs to the xanthine dehydrogenase family.

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 FAD-binding PCMH-type domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Peroxisome
Secreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   Ligand2Fe-2S
FAD
Flavoprotein
Iron
Iron-sulfur
Metal-binding
Molybdenum
NAD
   Molecular functionOxidoreductase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 18386220. Source: UniProtKB

lactation

Inferred from electronic annotation. Source: Ensembl

negative regulation of endothelial cell differentiation

Inferred from direct assay PubMed 18386220. Source: UniProtKB

negative regulation of endothelial cell proliferation

Inferred from direct assay PubMed 18386220. Source: UniProtKB

negative regulation of gene expression

Inferred from direct assay PubMed 18386220. Source: UniProtKB

negative regulation of protein kinase B signaling

Inferred from direct assay PubMed 18386220. Source: UniProtKB

negative regulation of protein phosphorylation

Inferred from direct assay PubMed 18386220. Source: UniProtKB

negative regulation of vascular endothelial growth factor signaling pathway

Inferred from direct assay PubMed 18386220. Source: UniProtKB

negative regulation of vasculogenesis

Inferred from direct assay PubMed 18386220. Source: UniProtKB

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

positive regulation of p38MAPK cascade

Inferred from direct assay PubMed 18386220. Source: UniProtKB

positive regulation of reactive oxygen species metabolic process

Inferred from direct assay PubMed 18386220. Source: UniProtKB

purine nucleobase metabolic process

Traceable author statement. Source: Reactome

purine nucleotide catabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

xanthine catabolic process

Inferred from direct assay Ref.10Ref.5. Source: UniProtKB

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

peroxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function2 iron, 2 sulfur cluster binding

Inferred from direct assay Ref.10. Source: UniProtKB

UDP-N-acetylmuramate dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Inferred from electronic annotation. Source: InterPro

flavin adenine dinucleotide binding

Inferred from direct assay Ref.10. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: InterPro

molybdopterin cofactor binding

Inferred from direct assay Ref.10. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.10. Source: UniProtKB

xanthine dehydrogenase activity

Inferred from direct assay Ref.5. Source: UniProtKB

xanthine oxidase activity

Inferred from direct assay Ref.10Ref.5. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 13331332Xanthine dehydrogenase/oxidase
PRO_0000166084

Regions

Domain4 – 91882Fe-2S ferredoxin-type
Domain229 – 414186FAD-binding PCMH-type
Nucleotide binding257 – 2648FAD
Nucleotide binding347 – 3515FAD

Sites

Active site12621Proton acceptor
Metal binding431Iron-sulfur (2Fe-2S) 1
Metal binding481Iron-sulfur (2Fe-2S) 1
Metal binding511Iron-sulfur (2Fe-2S) 1
Metal binding731Iron-sulfur (2Fe-2S) 1
Metal binding1131Iron-sulfur (2Fe-2S) 2
Metal binding1161Iron-sulfur (2Fe-2S) 2
Metal binding1481Iron-sulfur (2Fe-2S) 2
Metal binding1501Iron-sulfur (2Fe-2S) 2
Metal binding7681Molybdenum
Metal binding7991Molybdenum; via carbonyl oxygen
Metal binding9131Molybdenum; via amide nitrogen
Metal binding10801Molybdenum; via amide nitrogen
Binding site3371FAD
Binding site3601FAD
Binding site4041FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site4221FAD
Binding site8031Substrate By similarity
Binding site8811Substrate
Binding site9151Substrate By similarity
Binding site10111Substrate

Amino acid modifications

Glycosylation10741N-linked (GlcNAc...) Ref.9
Disulfide bond509 ↔ 1318In oxidase form Ref.11
Disulfide bond536 ↔ 993In oxidase form Ref.11

Natural variations

Natural variant1331E → K. Ref.6
Corresponds to variant rs45447191 [ dbSNP | Ensembl ].
VAR_023976
Natural variant1491R → C in XU1. Ref.12
VAR_045900
Natural variant1721G → R. Ref.3 Ref.6
Corresponds to variant rs45523133 [ dbSNP | Ensembl ].
VAR_023977
Natural variant2351T → M. Ref.6
Corresponds to variant rs45469499 [ dbSNP | Ensembl ].
VAR_023978
Natural variant3951K → M. Ref.6
Corresponds to variant rs34929837 [ dbSNP | Ensembl ].
VAR_023979
Natural variant5551P → S. Ref.6
Corresponds to variant rs45577338 [ dbSNP | Ensembl ].
VAR_023980
Natural variant5841D → A. Ref.6
Corresponds to variant rs45491693 [ dbSNP | Ensembl ].
VAR_023981
Natural variant6071R → Q. Ref.6
Corresponds to variant rs45442092 [ dbSNP | Ensembl ].
VAR_023982
Natural variant6171K → N. Ref.6
Corresponds to variant rs45442398 [ dbSNP | Ensembl ].
VAR_023983
Natural variant6231T → I. Ref.6
Corresponds to variant rs45448694 [ dbSNP | Ensembl ].
VAR_023984
Natural variant6461I → V. Ref.6
Corresponds to variant rs17323225 [ dbSNP | Ensembl ].
VAR_023985
Natural variant7031I → V. Ref.6
Corresponds to variant rs17011368 [ dbSNP | Ensembl ].
VAR_023986
Natural variant7631L → F in a breast cancer sample; somatic mutation. Ref.14
VAR_035899
Natural variant7911R → G in a breast cancer sample; somatic mutation. Ref.14
VAR_035900
Natural variant9101T → M. Ref.6
Corresponds to variant rs669884 [ dbSNP | Ensembl ].
VAR_023987
Natural variant10911V → L. Ref.6
Corresponds to variant rs45619033 [ dbSNP | Ensembl ].
VAR_023988
Natural variant11091N → T. Ref.6
Corresponds to variant rs45547640 [ dbSNP | Ensembl ].
VAR_023989
Natural variant11501P → R. Ref.7
Corresponds to variant rs1042036 [ dbSNP | Ensembl ].
VAR_045901
Natural variant11761R → C. Ref.6
Corresponds to variant rs45624433 [ dbSNP | Ensembl ].
VAR_023990
Natural variant12961R → W. Ref.6
Corresponds to variant rs45564939 [ dbSNP | Ensembl ].
VAR_023991

Experimental info

Mutagenesis8031E → V: Strongly decreased activity towards xanthine and hypoxanthine. Increased affinity and activity towards aromatic aldehydes.
Mutagenesis8811R → M: Abolishes xanthine oxidase activity.
Sequence conflict2591V → E in AAA75287. Ref.3
Sequence conflict333 – 3342QL → HV in AAA75287. Ref.3
Sequence conflict4951H → Q in AAA75287. Ref.3
Sequence conflict515 – 5173FFF → LLL in AAA75287. Ref.3

Secondary structure

............................................................................................................................................................................................................... 1333
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P47989 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 806FF2C7413F84C5

FASTA1,333146,424
        10         20         30         40         50         60 
MTADKLVFFV NGRKVVEKNA DPETTLLAYL RRKLGLSGTK LGCGEGGCGA CTVMLSKYDR 

        70         80         90        100        110        120 
LQNKIVHFSA NACLAPICSL HHVAVTTVEG IGSTKTRLHP VQERIAKSHG SQCGFCTPGI 

       130        140        150        160        170        180 
VMSMYTLLRN QPEPTMEEIE NAFQGNLCRC TGYRPILQGF RTFARDGGCC GGDGNNPNCC 

       190        200        210        220        230        240 
MNQKKDHSVS LSPSLFKPEE FTPLDPTQEP IFPPELLRLK DTPRKQLRFE GERVTWIQAS 

       250        260        270        280        290        300 
TLKELLDLKA QHPDAKLVVG NTEIGIEMKF KNMLFPMIVC PAWIPELNSV EHGPDGISFG 

       310        320        330        340        350        360 
AACPLSIVEK TLVDAVAKLP AQKTEVFRGV LEQLRWFAGK QVKSVASVGG NIITASPISD 

       370        380        390        400        410        420 
LNPVFMASGA KLTLVSRGTR RTVQMDHTFF PGYRKTLLSP EEILLSIEIP YSREGEYFSA 

       430        440        450        460        470        480 
FKQASRREDD IAKVTSGMRV LFKPGTTEVQ ELALCYGGMA NRTISALKTT QRQLSKLWKE 

       490        500        510        520        530        540 
ELLQDVCAGL AEELHLPPDA PGGMVDFRCT LTLSFFFKFY LTVLQKLGQE NLEDKCGKLD 

       550        560        570        580        590        600 
PTFASATLLF QKDPPADVQL FQEVPKGQSE EDMVGRPLPH LAADMQASGE AVYCDDIPRY 

       610        620        630        640        650        660 
ENELSLRLVT STRAHAKIKS IDTSEAKKVP GFVCFISADD VPGSNITGIC NDETVFAKDK 

       670        680        690        700        710        720 
VTCVGHIIGA VVADTPEHTQ RAAQGVKITY EELPAIITIE DAIKNNSFYG PELKIEKGDL 

       730        740        750        760        770        780 
KKGFSEADNV VSGEIYIGGQ EHFYLETHCT IAVPKGEAGE MELFVSTQNT MKTQSFVAKM 

       790        800        810        820        830        840 
LGVPANRIVV RVKRMGGGFG GKETRSTVVS TAVALAAYKT GRPVRCMLDR DEDMLITGGR 

       850        860        870        880        890        900 
HPFLARYKVG FMKTGTVVAL EVDHFSNVGN TQDLSQSIME RALFHMDNCY KIPNIRGTGR 

       910        920        930        940        950        960 
LCKTNLPSNT AFRGFGGPQG MLIAECWMSE VAVTCGMPAE EVRRKNLYKE GDLTHFNQKL 

       970        980        990       1000       1010       1020 
EGFTLPRCWE ECLASSQYHA RKSEVDKFNK ENCWKKRGLC IIPTKFGISF TVPFLNQAGA 

      1030       1040       1050       1060       1070       1080 
LLHVYTDGSV LLTHGGTEMG QGLHTKMVQV ASRALKIPTS KIYISETSTN TVPNTSPTAA 

      1090       1100       1110       1120       1130       1140 
SVSADLNGQA VYAACQTILK RLEPYKKKNP SGSWEDWVTA AYMDTVSLSA TGFYRTPNLG 

      1150       1160       1170       1180       1190       1200 
YSFETNSGNP FHYFSYGVAC SEVEIDCLTG DHKNLRTDIV MDVGSSLNPA IDIGQVEGAF 

      1210       1220       1230       1240       1250       1260 
VQGLGLFTLE ELHYSPEGSL HTRGPSTYKI PAFGSIPIEF RVSLLRDCPN KKAIYASKAV 

      1270       1280       1290       1300       1310       1320 
GEPPLFLAAS IFFAIKDAIR AARAQHTGNN VKELFRLDSP ATPEKIRNAC VDKFTTLCVT 

      1330 
GVPENCKPWS VRV 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene."
Ichida K., Amaya Y., Noda K., Minoshima S., Hosoya T., Sakai O., Shimizu N., Nishino T.
Gene 133:279-284(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]Ichida K.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 191; 231 AND 1150.
[3]"Molecular cloning, tissue expression of human xanthine dehydrogenase."
Xu P., Huecksteadt T.P., Harrison R., Hoidal J.R.
Biochem. Biophys. Res. Commun. 199:998-1004(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-172.
Tissue: Liver.
[4]Erratum
Xu P., Huecksteadt T.P., Harrison R., Hoidal J.R.
Biochem. Biophys. Res. Commun. 215:429-429(1995) [PubMed] [Europe PMC] [Abstract]
[5]"Cloning and expression in vitro of human xanthine dehydrogenase/oxidase."
Saksela M., Raivio K.O.
Biochem. J. 315:235-239(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY.
Tissue: Small intestine.
[6]NIEHS SNPs program
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-133; ARG-172; MET-235; MET-395; SER-555; ALA-584; GLN-607; ASN-617; ILE-623; VAL-646; VAL-703; MET-910; LEU-1091; THR-1109; CYS-1176 AND TRP-1296.
[7]"Identification of two mutations in human xanthine dehydrogenase gene responsible for classical type I xanthinuria."
Ichida K., Amaya Y., Kamatani N., Nishino T., Hosoya T., Sakai O.
J. Clin. Invest. 99:2391-2397(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN XU1, VARIANT ARG-1150.
[8]"XDH gene mutation is the underlying cause of classical xanthinuria: a second report."
Levartovsky D., Lagziel A., Sperling O., Liberman U., Yaron M., Hosoya T., Ichida K., Peretz H.
Kidney Int. 57:2215-2220(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN XU1.
[9]"Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1074.
Tissue: Milk.
[10]"Human xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site: roles of active site residues in binding and activation of purine substrate."
Yamaguchi Y., Matsumura T., Ichida K., Okamoto K., Nishino T.
J. Biochem. 141:513-524(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF MUTANT VAL-803 IN COMPLEX WITH FAD; 2FE-2S IRON-SULFUR CENTERS; SALICYLATE; MOLYBDOPTERIN AND CALCIUM IONS, COFACTOR, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT.
[11]"Human milk xanthine dehydrogenase is incompletely converted to the oxidase form in the absence of proteolysis. A structural explanation."
Pearson A.R., Godber B.L.J., Eisenthal R., Taylor G.L., Harrison R.
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (3.59 ANGSTROMS) IN COMPLEX WITH FAD AND IRON-SULFUR CENTERS, TISSUE SPECIFICITY, ENZYME REGULATION, DISULFIDE BONDS.
[12]"Identification of a new point mutation in the human xanthine dehydrogenase gene responsible for a case of classical type I xanthinuria."
Sakamoto N., Yamamoto T., Moriwaki Y., Teranishi T., Toyoda M., Onishi Y., Kuroda S., Sakaguchi K., Fujisawa T., Maeda M., Hada T.
Hum. Genet. 108:279-283(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT XU1 CYS-149.
[13]"Mutational analysis of the xanthine dehydrogenase gene in a Turkish family with autosomal recessive classical xanthinuria."
Gok F., Ichida K., Topaloglu R.
Nephrol. Dial. Transplant. 18:2278-2283(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN XU1.
[14]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] PHE-763 AND GLY-791.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D11456 mRNA. Translation: BAA02013.2.
U06117 mRNA. Translation: AAA75287.1.
U39487 mRNA. Translation: AAB08399.1.
DQ089481 Genomic DNA. Translation: AAY68219.1.
PIRXOHUDH. S66573.
RefSeqNP_000370.2. NM_000379.3.
UniGeneHs.250.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CKJX-ray3.59A/B/C/D2-1332[»]
2E1QX-ray2.60A/B/C/D2-1332[»]
ProteinModelPortalP47989.
SMRP47989. Positions 3-164, 195-528, 572-1316.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113335. 4 interactions.
IntActP47989. 2 interactions.
STRING9606.ENSP00000368727.

Chemistry

BindingDBP47989.
ChEMBLCHEMBL1929.
DrugBankDB00437. Allopurinol.
DB01136. Carvedilol.
DB00694. Daunorubicin.
DB00746. Deferoxamine.
DB01189. Desflurane.
DB00170. Menadione.
DB01033. Mercaptopurine.
DB00563. Methotrexate.
DB00157. NADH.
DB00336. Nitrofurazone.
DB01113. Papaverine.
DB01168. Procarbazine.
DB00339. Pyrazinamide.
DB00049. Rasburicase.
DB00127. Spermine.
DB00831. Trifluoperazine.
DB00163. Vitamin E.
GuidetoPHARMACOLOGY2646.

PTM databases

PhosphoSiteP47989.

Polymorphism databases

DMDM2506326.

Proteomic databases

PaxDbP47989.
PeptideAtlasP47989.
PRIDEP47989.

Protocols and materials databases

DNASU7498.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379416; ENSP00000368727; ENSG00000158125.
GeneID7498.
KEGGhsa:7498.
UCSCuc002rnv.1. human.

Organism-specific databases

CTD7498.
GeneCardsGC02M031470.
H-InvDBHIX0117690.
HGNCHGNC:12805. XDH.
HPACAB009518.
MIM278300. phenotype.
607633. gene.
neXtProtNX_P47989.
Orphanet93601. Xanthinuria type I.
PharmGKBPA37404.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4630.
HOGENOMHOG000191197.
HOVERGENHBG004182.
InParanoidP47989.
KOK00106.
OMAFHMENSY.
OrthoDBEOG7QRQSZ.
PhylomeDBP47989.
TreeFamTF353036.

Enzyme and pathway databases

BioCycMetaCyc:HS08270-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP47989.

Gene expression databases

ArrayExpressP47989.
BgeeP47989.
CleanExHS_XDH.
GenevestigatorP47989.

Family and domain databases

Gene3D1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
IPR022407. OxRdtase_Mopterin_BS.
IPR014307. Xanthine_DH_ssu.
[Graphical view]
PfamPF01315. 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.
[Graphical view]
PIRSFPIRSF000127. Xanthine_DH. 1 hit.
SMARTSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsTIGR02963. xanthine_xdhA. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSXDH. human.
EvolutionaryTraceP47989.
GeneWikiXanthine_dehydrogenase.
GenomeRNAi7498.
NextBio29364.
PROP47989.
SOURCESearch...

Entry information

Entry nameXDH_HUMAN
AccessionPrimary (citable) accession number: P47989
Secondary accession number(s): Q16681, Q16712, Q4PJ16
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 148 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM