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Protein

Xanthine dehydrogenase/oxidase

Gene

Xdh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Catalytic activityi

Xanthine + NAD+ + H2O = urate + NADH.By similarity
Hypoxanthine + NAD+ + H2O = xanthine + NADH.By similarity
Xanthine + H2O + O2 = urate + H2O2.By similarity

Cofactori

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterBy similarityNote: Binds 2 [2Fe-2S] clusters.By similarity
  • FADBy similarity
  • Mo-molybdopterinBy similarityNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

Enzyme 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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi46Iron-sulfur 1By similarity1
Metal bindingi51Iron-sulfur 1By similarity1
Metal bindingi54Iron-sulfur 1By similarity1
Metal bindingi76Iron-sulfur 1By similarity1
Metal bindingi115Iron-sulfur 2By similarity1
Metal bindingi118Iron-sulfur 2By similarity1
Metal bindingi150Iron-sulfur 2By similarity1
Metal bindingi152Iron-sulfur 2By similarity1
Binding sitei339FADBy similarity1
Binding sitei362FADBy similarity1
Binding sitei406FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei424FADBy similarity1
Metal bindingi770MolybdenumBy similarity1
Metal bindingi801Molybdenum; via carbonyl oxygenBy similarity1
Binding sitei805SubstrateBy similarity1
Binding sitei883SubstrateBy similarity1
Metal bindingi915Molybdenum; via amide nitrogenBy similarity1
Binding sitei917SubstrateBy similarity1
Binding sitei1013Substrate; via amide nitrogenBy similarity1
Metal bindingi1082Molybdenum; via amide nitrogenBy similarity1
Active sitei1264Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi259 – 266FADBy similarity8
Nucleotide bindingi349 – 353FADBy similarity5

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14019.
ReactomeiR-MMU-74259. Purine catabolism.
SABIO-RKQ00519.

Names & Taxonomyi

Protein namesi
Recommended name:
Xanthine dehydrogenase/oxidase
Including the following 2 domains:
Xanthine dehydrogenase (EC:1.17.1.4By similarity)
Short name:
XD
Xanthine oxidase (EC:1.17.3.2By similarity)
Short name:
XO
Alternative name(s):
Xanthine oxidoreductase
Short name:
XOR
Gene namesi
Name:Xdh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:98973. Xdh.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GO_Central
  • extracellular space Source: MGI
  • peroxisome Source: UniProtKB-SubCell
  • sarcoplasmic reticulum Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001660852 – 1335Xanthine dehydrogenase/oxidaseAdd BLAST1334

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi538 ↔ 995In oxidase formBy similarity
Glycosylationi1076N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ00519.
MaxQBiQ00519.
PaxDbiQ00519.
PeptideAtlasiQ00519.
PRIDEiQ00519.

PTM databases

iPTMnetiQ00519.
PhosphoSitePlusiQ00519.
SwissPalmiQ00519.

Expressioni

Inductioni

By interferon.

Gene expression databases

BgeeiENSMUSG00000024066.
CleanExiMM_XDH.
GenevisibleiQ00519. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with BTN1A1.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ00519. 2 interactors.
MINTiMINT-1866314.
STRINGi10090.ENSMUSP00000024866.

Structurei

3D structure databases

ProteinModelPortaliQ00519.
SMRiQ00519.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 942Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST88
Domaini231 – 416FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST186

Sequence similaritiesi

Belongs to the xanthine dehydrogenase family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0430. Eukaryota.
COG4630. LUCA.
COG4631. LUCA.
GeneTreeiENSGT00390000003772.
HOGENOMiHOG000191197.
HOVERGENiHBG004182.
InParanoidiQ00519.
KOiK00106.
OMAiCERAMTH.
OrthoDBiEOG091G01AW.
TreeFamiTF353036.

Family and domain databases

Gene3Di1.10.150.120. 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.
InterProiIPR002888. 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.
IPR014309. Xanthine_DH_Mopterin-bd_su.
IPR014307. Xanthine_DH_ssu.
[Graphical view]
PfamiPF01315. 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]
PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
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.
TIGR02965. xanthine_xdhB. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q00519-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRTTVDELV FFVNGKKVVE KNADPETTLL VYLRRKLGLC GTKLGCGEGG
60 70 80 90 100
CGACTVMISK YDRLQNKIVH FSVNACLTPI CSLHHVAVTT VEGIGNTKKL
110 120 130 140 150
HPVQERIAKS HGSQCGFCTP GIVMSMYTLL RNKPEPTVEE IENAFQGNLC
160 170 180 190 200
RCTGYRPILQ GFRTFAKDGG CCGGSGNNPN CCMSQTKDQT IAPSSSLFNP
210 220 230 240 250
EDFKPLDPTQ EPIFPPELLR LKDTPRKTLR FEGERVTWIQ VSTMEELLDL
260 270 280 290 300
KAQHPDAKLV VGNTEIGIEM KFKNMLFPLI ICPAWILELT SVAHGPEGIS
310 320 330 340 350
FGAACPLSLV ESVLADAIAT LPEQRTEVFR GVMEQLRWFA GKQVKSVASI
360 370 380 390 400
GGNIITASPI SDLNPVLMAS RAKLTLASRG TKRTVWMDHT FFPGYRRTLL
410 420 430 440 450
SPEEILVSIV IPYSRKGEFF SAFKQASRRE DDIAKVTSGM RVLFKPGTTE
460 470 480 490 500
VQELSLCFGG MADRTVSALK TTPKQLSKSW NEELLQDVCA GLAEELHLAP
510 520 530 540 550
DAPGGMVEFR RTLTLSFFFK FYLTVLQKLG RADLEGMCGK LDPTFASATL
560 570 580 590 600
LFQKDPPANV QLFQEVPKGQ SEEDMVGRPM PHLAADMQAS GEAVYCDDIP
610 620 630 640 650
RYENELSLRL VTSTRAHAKI MSIDTSEAKK VPGFVCFLTS EDVPGSNITG
660 670 680 690 700
IFNDETVFAK DEVTCVGHII GAVVADTPEH AHRAARGVKI TYEDLPAIIT
710 720 730 740 750
IQDAIKNNSF YGPEVKIEKG DLKKGFSEAD NVVSGELYIG GQEHFYLETH
760 770 780 790 800
CTIAVPKGEA GEMELFVSTQ NTMKTQSFIA KMLGVPDNRI VVRVKRMGGG
810 820 830 840 850
FGGKETRSTL ISTAVALAAY KTGRPVRCML DRDEDMLITG GRHPFLAKYK
860 870 880 890 900
VGFMKTGTIV ALEVAHFSNG GNSEDLSRSI MERAVFHMDN AYKIPNIRGT
910 920 930 940 950
GRICKTNLPS NTAFRGFGGP QGMLIAEYWM SEVAVTCGLP AEEVRRKNMY
960 970 980 990 1000
KEGDLTHFNQ KLEGFTLPRC WDECIASSQY QARKMEVEKF NRENCWKKRG
1010 1020 1030 1040 1050
LCIIPTKFGI SFTLSFLNQG GALVHVYTDG SVLLTHGGTE MGQGLHTKMV
1060 1070 1080 1090 1100
QVASRALKIP TSKIHITETS TNTVPNTSPT AASASADLNG QAIYEACQTI
1110 1120 1130 1140 1150
LKRLEPFKKK NPSGSWESWV MDAYTSAVSL SATGFYKTPN LGYSFETNSG
1160 1170 1180 1190 1200
NPFHYFSYGV ACSEVEIDCL TGDHKNLRTD IVMDVGSSLN PAIDIGQVEG
1210 1220 1230 1240 1250
AFVQGLGLFT MEELHYSPEG SLHTRGPSTY KIPAFGSIPI EFRVSLLRDC
1260 1270 1280 1290 1300
PNKRAIYASK AVGEPPLFLA SSIFFAIKDA IRAARAQHGD SNAKQLFQLD
1310 1320 1330
SPATPEKIRN ACVDQFTTLC ATGTPENCKS WSVRI
Length:1,335
Mass (Da):146,562
Last modified:July 27, 2011 - v5
Checksum:i56AD3E0C75E00F98
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti241V → I in CAA44705 (PubMed:1590774).Curated1
Sequence conflicti621M → T in CAA52997 (PubMed:7835888).Curated1
Sequence conflicti1247L → V in CAA52997 (PubMed:7835888).Curated1
Sequence conflicti1247L → V in CAA44705 (PubMed:1590774).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75129
, X75128, X75127, X75126, X75125, X75124, X75123, X75122, X75121, X75120, X75119, X75130, X75131, X75132, X75133, X75134, X75135, X75136, X75137, X75138, X75139, X75140, X75141, X75142, X75143, X75151, X75152, X75153, X75154, X75144, X75145, X75146, X75147, X75148, X75149, X75150 Genomic DNA. Translation: CAA52997.1.
X62932 mRNA. Translation: CAA44705.1.
AC159187 Genomic DNA. No translation available.
CT025731 Genomic DNA. No translation available.
CCDSiCCDS28967.1.
PIRiI48374. XOMSDH.
RefSeqiNP_035853.2. NM_011723.3.
UniGeneiMm.11223.

Genome annotation databases

EnsembliENSMUST00000024866; ENSMUSP00000024866; ENSMUSG00000024066.
GeneIDi22436.
KEGGimmu:22436.
UCSCiuc008dno.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75129
, X75128, X75127, X75126, X75125, X75124, X75123, X75122, X75121, X75120, X75119, X75130, X75131, X75132, X75133, X75134, X75135, X75136, X75137, X75138, X75139, X75140, X75141, X75142, X75143, X75151, X75152, X75153, X75154, X75144, X75145, X75146, X75147, X75148, X75149, X75150 Genomic DNA. Translation: CAA52997.1.
X62932 mRNA. Translation: CAA44705.1.
AC159187 Genomic DNA. No translation available.
CT025731 Genomic DNA. No translation available.
CCDSiCCDS28967.1.
PIRiI48374. XOMSDH.
RefSeqiNP_035853.2. NM_011723.3.
UniGeneiMm.11223.

3D structure databases

ProteinModelPortaliQ00519.
SMRiQ00519.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ00519. 2 interactors.
MINTiMINT-1866314.
STRINGi10090.ENSMUSP00000024866.

PTM databases

iPTMnetiQ00519.
PhosphoSitePlusiQ00519.
SwissPalmiQ00519.

Proteomic databases

EPDiQ00519.
MaxQBiQ00519.
PaxDbiQ00519.
PeptideAtlasiQ00519.
PRIDEiQ00519.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024866; ENSMUSP00000024866; ENSMUSG00000024066.
GeneIDi22436.
KEGGimmu:22436.
UCSCiuc008dno.2. mouse.

Organism-specific databases

CTDi7498.
MGIiMGI:98973. Xdh.

Phylogenomic databases

eggNOGiKOG0430. Eukaryota.
COG4630. LUCA.
COG4631. LUCA.
GeneTreeiENSGT00390000003772.
HOGENOMiHOG000191197.
HOVERGENiHBG004182.
InParanoidiQ00519.
KOiK00106.
OMAiCERAMTH.
OrthoDBiEOG091G01AW.
TreeFamiTF353036.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14019.
ReactomeiR-MMU-74259. Purine catabolism.
SABIO-RKQ00519.

Miscellaneous databases

ChiTaRSiXdh. mouse.
PROiQ00519.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024066.
CleanExiMM_XDH.
GenevisibleiQ00519. MM.

Family and domain databases

Gene3Di1.10.150.120. 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.
InterProiIPR002888. 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.
IPR014309. Xanthine_DH_Mopterin-bd_su.
IPR014307. Xanthine_DH_ssu.
[Graphical view]
PfamiPF01315. 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]
PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
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.
TIGR02965. xanthine_xdhB. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXDH_MOUSE
AccessioniPrimary (citable) accession number: Q00519
Secondary accession number(s): E9QLM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 155 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.