Reviewed, UniProtKB/Swiss-Prot P47989 (XDH_HUMAN)

Names and origin

Protein names

Recommended name:
    Xanthine dehydrogenase/oxidase
Including the following 2 domains:
    1- Recommended name:
            Xanthine dehydrogenase
                Short name=XD
              EC=1.17.1.4
    2- Recommended name:
            Xanthine oxidase
                Short name=XO
              EC=1.17.3.2
        Alternative name(s):
            Xanthine oxidoreductase

Gene names

Name:	XDH
Synonyms:	XDHA

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1333 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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).
Catalytic activity	Hypoxanthine + NAD+ + H2O = xanthine + NADH. Xanthine + H2O + O2 = urate + H2O2.
Cofactor	Binds 2 2Fe-2S clusters. FAD. Binds 1 molybdenum ion (molybdopterin) per subunit.
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.
Subunit structure	Homodimer. Interacts with BTN1A1 By similarity.
Subcellular location	Cytoplasm By similarity. Peroxisome By similarity. Secreted.
Tissue specificity	Detected in milk (at protein level).
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	Defects in XDH are the cause of xanthinuria type 1 (XU1) [MIM:278300]. Xanthinuria is 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. XU1 is due to isolated xanthine dehydrogenase. XU1 patients can metabolize allopurinol. Ref.8 Ref.9 Ref.13 Ref.14
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 component	Cytoplasm Peroxisome Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW xanthine catabolic process Ref.11 Inferred from direct assay. Source: UniProtKB
Cellular component	cytosol Ref.5 Inferred from Experiment. Source: Reactome peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2 iron, 2 sulfur cluster binding Ref.11 Inferred from direct assay. Source: UniProtKB FAD binding Ref.11 Inferred from direct assay. Source: UniProtKB electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW molybdenum ion binding Inferred from electronic annotation. Source: UniProtKB-KW molybdopterin cofactor binding Ref.11 Inferred from direct assay. Source: UniProtKB protein homodimerization activity Ref.11 Inferred from physical interaction. Source: UniProtKB xanthine dehydrogenase activity Ref.1 Traceable author statement. Source: ProtInc xanthine oxidase activity Ref.5 Ref.11 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 1333

1332

Xanthine dehydrogenase/oxidase

PRO_0000166084

Regions

Domain

4 – 91

88

2Fe-2S ferredoxin-type

Domain

229 – 414

186

FAD-binding PCMH-type

Nucleotide binding

257 – 264

8

FAD

Nucleotide binding

347 – 351

5

FAD

Sites

Active site

1262

1

Proton acceptor

Metal binding

43

1

Iron-sulfur (2Fe-2S) 1

Metal binding

48

1

Iron-sulfur (2Fe-2S) 1

Metal binding

51

1

Iron-sulfur (2Fe-2S) 1

Metal binding

73

1

Iron-sulfur (2Fe-2S) 1

Metal binding

113

1

Iron-sulfur (2Fe-2S) 2

Metal binding

116

1

Iron-sulfur (2Fe-2S) 2

Metal binding

148

1

Iron-sulfur (2Fe-2S) 2

Metal binding

150

1

Iron-sulfur (2Fe-2S) 2

Metal binding

768

1

Molybdenum

Metal binding

799

1

Molybdenum; via carbonyl oxygen

Metal binding

913

1

Molybdenum; via amide nitrogen

Metal binding

1080

1

Molybdenum; via amide nitrogen

Binding site

337

1

FAD

Binding site

360

1

FAD

Binding site

404

1

FAD; via amide nitrogen and carbonyl oxygen By similarity

Binding site

422

1

FAD

Binding site

803

1

Substrate By similarity

Binding site

881

1

Substrate

Binding site

915

1

Substrate By similarity

Binding site

1011

1

Substrate

Amino acid modifications

Modified residue

222

1

Phosphothreonine Ref.7

Glycosylation

1074

1

N-linked (GlcNAc...) Ref.10

Disulfide bond

509 ↔ 1318

In oxidase form

Disulfide bond

536 ↔ 993

In oxidase form

Natural variations

Natural variant

133

1

E → K: dbSNP rs45447191. Ref.6

VAR_023976

Natural variant

149

1

R → C in XU1. Ref.13

VAR_045900

Natural variant

172

1

G → R: dbSNP rs45523133. Ref.6 Ref.3

VAR_023977

Natural variant

235

1

T → M: dbSNP rs45469499. Ref.6

VAR_023978

Natural variant

395

1

K → M: dbSNP rs34929837. Ref.6

VAR_023979

Natural variant

555

1

P → S: dbSNP rs45577338. Ref.6

VAR_023980

Natural variant

584

1

D → A: dbSNP rs45491693. Ref.6

VAR_023981

Natural variant

607

1

R → Q: dbSNP rs45442092. Ref.6

VAR_023982

Natural variant

617

1

K → N: dbSNP rs45442398. Ref.6

VAR_023983

Natural variant

623

1

T → I: dbSNP rs45448694. Ref.6

VAR_023984

Natural variant

646

1

I → V: dbSNP rs17323225. Ref.6

VAR_023985

Natural variant

703

1

I → V: dbSNP rs17011368. Ref.6

VAR_023986

Natural variant

763

1

L → F in a breast cancer sample; somatic mutation. Ref.15

VAR_035899

Natural variant

791

1

R → G in a breast cancer sample; somatic mutation. Ref.15

VAR_035900

Natural variant

910

1

T → M

VAR_023987

Natural variant

1091

1

V → L: dbSNP rs45619033. Ref.6

VAR_023988

Natural variant

1109

1

N → T: dbSNP rs45547640. Ref.6

VAR_023989

Natural variant

1150

1

P → R: dbSNP rs1042036. Ref.8

VAR_045901

Natural variant

1176

1

R → C: dbSNP rs45624433. Ref.6

VAR_023990

Natural variant

1296

1

R → W: dbSNP rs45564939. Ref.6

VAR_023991

Experimental info

Mutagenesis

803

1

E → V: Strongly decreased activity towards xanthine and hypoxanthine. Increased affinity and activity towards aromatic aldehydes.

Mutagenesis

881

1

R → M: Abolishes xanthine oxidase activity.

Sequence conflict

259

1

V → E in AAA75287. Ref.3

Sequence conflict

333 – 334

2

QL → HV in AAA75287. Ref.3

Sequence conflict

495

1

H → Q in AAA75287. Ref.3

Sequence conflict

515 – 517

3

FFF → LLL in AAA75287. Ref.3

Secondary structure

1

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1333

Helix Strand Turn

Details...

Beta strand

6 – 10

5

Beta strand

13 – 17

5

Helix

26 – 32

7

Beta strand

44 – 48

5

Beta strand

52 – 59

8

Turn

60 – 63

4

Beta strand

64 – 71

8

Turn

72 – 74

3

Helix

77 – 79

3

Beta strand

84 – 86

3

Helix

88 – 90

3

Helix

100 – 107

8

Helix

117 – 130

14

Helix

136 – 141

6

Turn

142 – 145

4

Beta strand

149 – 151

3

Helix

154 – 160

7

Helix

161 – 163

3

Helix

198 – 200

3

Helix

206 – 208

3

Helix

214 – 218

5

Beta strand

227 – 230

4

Beta strand

235 – 238

4

Helix

242 – 251

10

Helix

264 – 270

7

Beta strand

276 – 280

5

Helix

285 – 288

4

Beta strand

290 – 292

3

Beta strand

294 – 300

7

Helix

305 – 318

14

Helix

321 – 323

3

Helix

325 – 335

11

Helix

340 – 345

6

Helix

348 – 354

7

Helix

362 – 367

6

Beta strand

371 – 375

5

Beta strand

380 – 384

5

Helix

387 – 389

3

Beta strand

403 – 410

8

Beta strand

416 – 423

8

Beta strand

425 – 429

5

Beta strand

433 – 442

10

Beta strand

448 – 465

18

Helix

467 – 471

5

Turn

472 – 475

4

Beta strand

477 – 479

3

Helix

480 – 493

14

Helix

505 – 529

25

Turn

541 – 543

3

Helix

544 – 547

4

Beta strand

556 – 560

5

Helix

583 – 587

5

Helix

594 – 596

3

Beta strand

604 – 610

7

Beta strand

612 – 622

11

Helix

626 – 628

3

Beta strand

632 – 637

6

Helix

638 – 640

3

Beta strand

645 – 648

4

Beta strand

653 – 656

4

Beta strand

659 – 661

3

Beta strand

667 – 675

9

Helix

676 – 684

9

Beta strand

687 – 692

6

Helix

699 – 705

7

Beta strand

708 – 718

11

Helix

720 – 726

7

Beta strand

728 – 737

10

Beta strand

749 – 754

6

Beta strand

761 – 765

5

Helix

770 – 781

12

Helix

785 – 787

3

Beta strand

788 – 793

6

Turn

799 – 802

4

Helix

807 – 820

14

Beta strand

824 – 827

4

Helix

830 – 837

8

Beta strand

843 – 851

9

Beta strand

857 – 871

15

Helix

875 – 884

10

Beta strand

893 – 903

11

Turn

913 – 916

4

Helix

917 – 935

19

Helix

939 – 945

7

Helix

965 – 976

12

Helix

978 – 991

14

Beta strand

993 – 1009

17

Helix

1013 – 1015

3

Beta strand

1017 – 1024

8

Beta strand

1030 – 1035

6

Beta strand

1039 – 1041

3

Helix

1043 – 1055

13

Helix

1059 – 1061

3

Turn

1069 – 1071

3

Helix

1083 – 1108

26

Helix

1114 – 1123

10

Beta strand

1129 – 1135

7

Turn

1143 – 1146

4

Beta strand

1152 – 1166

15

Turn

1167 – 1169

3

Beta strand

1172 – 1182

11

Helix

1189 – 1208

20

Turn

1225 – 1227

3

Helix

1233 – 1235

3

Beta strand

1238 – 1244

7

Helix

1254 – 1256

3

Helix

1263 – 1268

6

Helix

1269 – 1286

18

Helix

1303 – 1309

7

Helix

1315 – 1317

3

Sequences

	Sequence		Length	Mass (Da)
	P47989-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 806FF2C7413F84C5	FASTA	1,333	146,424
	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

References

	« Hide 'large scale' referencesShow '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: 8224915] [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: 8135849] [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: 7575623] [Abstract]
[5]	"Cloning and expression in vitro of human xanthine dehydrogenase/oxidase." Saksela M., Raivio K.O. Biochem. J. 315:235-239(1996) [PubMed: 8670112] [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]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-222, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"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: 9153281] [Abstract] Cited for: INVOLVEMENT IN XU1, VARIANT ARG-1150.
[9]	"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: 10844591] [Abstract] Cited for: INVOLVEMENT IN XU1.
[10]	"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: 18780401] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1074, MASS SPECTROMETRY. Tissue: Milk.
[11]	"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: 17301077] [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.
[12]	"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.
[13]	"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: 11379872] [Abstract] Cited for: VARIANT XU1 CYS-149.
[14]	"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: 14551354] [Abstract] Cited for: INVOLVEMENT IN XU1.
[15]	"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. , 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: 16959974] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] PHE-763 AND GLY-791.
+	Additional computationally mapped references.

Web resources

GeneReviews

NIEHS-SNPs

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.

IPI

IPI00244391.

PIR

XOHUDH. S66573.

RefSeq

NP_000370.2.

UniGene

Hs.250

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CKJ	X-ray	3.59	A/B/C/D	2-1332	[»]
2E1Q	X-ray	2.60	A/B/C/D	2-1332	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P47989.

PTM databases

PhosphoSite

P47989.

Proteomic databases

PeptideAtlas

P47989.

PRIDE

P47989.

Genome annotation databases

Ensembl

ENST00000379416; ENSP00000368727; ENSG00000158125; Homo sapiens. [Genome view]

GeneID

7498.

KEGG

hsa:7498.

NMPDR

fig|9606.3.peg.17717.

UCSC

uc002rnv.1. human.

Organism-specific databases

CTD

7498.

GeneCards

GC02M031470.

H-InvDB

HIX0023973.
HIX0030009.

HGNC

HGNC:12805. XDH.

HPA

CAB009518.

MIM

278300. phenotype.
607633. gene.

Orphanet

3467. Xanthinuria.

PharmGKB

PA37404.

GenAtlas

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Phylogenomic databases

eggNOG

prNOG09302.

HOGENOM

HBG386245.

HOVERGEN

P47989.

InParanoid

P47989.

OMA

ELALCYG.

OrthoDB

EOG9V722T.

PhylomeDB

P47989.

Enzyme and pathway databases

BRENDA

1.17.1.4. 247.
1.17.3.2. 247.

Reactome

REACT_1698. Metabolism of nucleotides.

Gene expression databases

ArrayExpress

P47989.

Bgee

P47989.

CleanEx

HS_XDH.

Genevestigator

P47989.

GermOnline

ENSG00000158125. Homo sapiens.

Family and domain databases

InterPro

IPR002888. 2Fe-2S_bd.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. b-grasp_ferredoxin-like.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR001041. Ferredoxin.
IPR002346. Mopterin_DH_FAD-bd.
IPR000572. OxRdtase_Mopterin-bd.
IPR014309. Xanthine_DH_Mopterin-bd_su.
IPR014307. Xanthine_DH_ssu.
[Graphical view]

Gene3D

G3DSA:3.30.365.10. Ald_xan_DH_mo_bd. 2 hits.
G3DSA:3.90.1170.50. Aldxan_DH_hamm. 1 hit.
G3DSA:3.30.390.50. CO_DH_flav_C. 1 hit.
G3DSA:3.30.465.10. CO_DH_flavoprot_FAD-bd_sub2. 1 hit.
G3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit.
G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.

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.
[Graphical view]

PIRSF

PIRSF000127. Xanthine_DH. 1 hit.

TIGRFAMs

TIGR02963. xanthine_xdhA. 1 hit.
TIGR02965. xanthine_xdhB. 1 hit.

PROSITE

PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

DrugBank

DB00437. 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.

NextBio

29364.

SOURCE

Search...

Entry information

Entry name

XDH_HUMAN

Accession

Primary (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:	February 9, 2010
This is version 108 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.