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Protein

Xanthine dehydrogenase/oxidase

Gene

XDH

Organism
Felis catus (Cat) (Felis silvestris catus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 bindingi43Iron-sulfur 1By similarity1
Metal bindingi48Iron-sulfur 1By similarity1
Metal bindingi51Iron-sulfur 1By similarity1
Metal bindingi73Iron-sulfur 1By similarity1
Metal bindingi113Iron-sulfur 2By similarity1
Metal bindingi116Iron-sulfur 2By similarity1
Metal bindingi148Iron-sulfur 2By similarity1
Metal bindingi150Iron-sulfur 2By similarity1
Binding sitei335FADBy similarity1
Binding sitei358FADBy similarity1
Binding sitei402FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei420FADBy similarity1
Metal bindingi766MolybdenumBy similarity1
Metal bindingi797Molybdenum; via carbonyl oxygenBy similarity1
Binding sitei801SubstrateBy similarity1
Binding sitei879SubstrateBy similarity1
Metal bindingi911Molybdenum; via amide nitrogenBy similarity1
Binding sitei913SubstrateBy similarity1
Binding sitei1009Substrate; via amide nitrogenBy similarity1
Metal bindingi1078Molybdenum; via amide nitrogenBy similarity1
Active sitei1260Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi257 – 264FADBy similarity8
Nucleotide bindingi345 – 349FADBy 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

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
OrganismiFelis catus (Cat) (Felis silvestris catus)
Taxonomic identifieri9685 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis
Proteomesi
  • UP000011712 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002461762 – 1331Xanthine dehydrogenase/oxidaseAdd BLAST1330

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi534 ↔ 991In oxidase formBy similarity
Glycosylationi1072N-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

Interactioni

Subunit structurei

Homodimer. Interacts with BTN1A1 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9685.ENSFCAP00000004209.

Structurei

3D structure databases

ProteinModelPortaliQ9MYW6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 912Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST88
Domaini229 – 412FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST184

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.
COG4631. LUCA.
HOVERGENiHBG004182.
InParanoidiQ9MYW6.
KOiK00106.

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.
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.
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.

Q9MYW6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTADELVFFV NGKKVVEKNA DPETTLLAYL RRKLGLSGTK LGCGEGGCGA
60 70 80 90 100
CTVMLSKYDR FQNKIVHFSA NACLAPICSL HHVAVTTVEG IGSTKSRLHP
110 120 130 140 150
VQERIAKSHG SQCGFCTPGI VMSMYTLLRN QPEPTIEEIE DAFQGNLCRC
160 170 180 190 200
TGYRPILQGF RTFARDGGCC GGSGNDLNCC MNQKTDHKIT LSPSLFNPEE
210 220 230 240 250
FTPLDPTQEP IFPPELLRLK DTPQKQLRFE GERVTWIQAS TLQELLDLKA
260 270 280 290 300
QDPEAKLVVG NTEIGIEMKF KNMLFPKMVC PAWIPEPVEH GPEGISFGAS
310 320 330 340 350
CPLSLVEKTL LDAVANLPAH QTEVFKGVLE QLRWFAGKQV KSVASIGGNI
360 370 380 390 400
ITASPISDLN PVFMASGAKL TIVSTGTRRT VRMDHTFFPA YRKTLLAPEE
410 420 430 440 450
ILLSIEIPYS REGEYFSAFK QASRREDDIA KVTSGMRVLF NPGTAQVKEL
460 470 480 490 500
ALCYGGMHDR TVSALQTTRK QISNFWNEEL LQNVCAGLAE ELSLAPDAPG
510 520 530 540 550
GMVEFRRTLT LSFFFKFYLT VLQKLGIQNS KDKCGKLDPT HASATLLFQK
560 570 580 590 600
DPPANVQLFQ EVPKGQCEED MVGRPLPHLA AAMQASGEAV YCDDIPRYEN
610 620 630 640 650
ELSLRLVTST RAHAKIKSID TSEAQKVPGF VCFISADDVP GSNITGIGND
660 670 680 690 700
EMVFAKDKVT CIGHIIGAVV TDTREHAQRA AQAVRITYED LPAIITIEDA
710 720 730 740 750
IAKDSFYEPE LKIEKGNLTK GFSEADNIVS GELYIGGQEH FYLETHCTIA
760 770 780 790 800
VPKGEAGEME LFVSTQNTTK TQSFVANMLG VPANRILVRV KRMGGGFGGK
810 820 830 840 850
ETRSTVVSTA VPLAAYKTGR PVRCMLDRDE DMLITGGRHP FLARYKVGFM
860 870 880 890 900
KTGRVVALKV EHYSNAGNTL DLSQSIMERA LFHMDNCYNI PNIRGTGRIC
910 920 930 940 950
KTNLPSNTAF RGFGGPQGML IAEHWMSEVA VTCGLPAEEV RRKNMYKEGD
960 970 980 990 1000
LTHFNQKLEG FTLPRCWEEC LASSQYHARK READKFNEEN CWKKRGLSII
1010 1020 1030 1040 1050
PTKFGISFTV PFLNQAGALV HVYTDGSVLL THGGTEMGQG LHTKMVQVAS
1060 1070 1080 1090 1100
RALKIPTSKI YISETSTNTV PNTSPTAASV STDINGQAVY EACQTILKRL
1110 1120 1130 1140 1150
EPFKKKNPSG SWEDWVTAAY LDAVSLSATG FYKTPNIGYS FETNSGNPFH
1160 1170 1180 1190 1200
YFSYGVACSE VEIDCLTGDH KNLRTDIVMD VGSSLNPAID IGQVEGAFVQ
1210 1220 1230 1240 1250
GLGLFTLEEL HYSPEGSLHT RGPSTYKIPA FGSIPSEFRV SLLRDCPNKK
1260 1270 1280 1290 1300
AIYASKAVGE PPLFLAASIF FAIKDAICAA RAGNPDCKTK KLFQLNSPAT
1310 1320 1330
PEKIRNACVD QFTRLCVTGT AESCKPWSVR V
Length:1,331
Mass (Da):146,122
Last modified:January 23, 2007 - v3
Checksum:i726C4F72C3B5FB09
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF286379 mRNA. Translation: AAF97949.1.
RefSeqiNP_001009217.1. NM_001009217.1.

Genome annotation databases

GeneIDi493692.
KEGGifca:493692.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF286379 mRNA. Translation: AAF97949.1.
RefSeqiNP_001009217.1. NM_001009217.1.

3D structure databases

ProteinModelPortaliQ9MYW6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9685.ENSFCAP00000004209.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi493692.
KEGGifca:493692.

Organism-specific databases

CTDi7498.

Phylogenomic databases

eggNOGiKOG0430. Eukaryota.
COG4631. LUCA.
HOVERGENiHBG004182.
InParanoidiQ9MYW6.
KOiK00106.

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.
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.
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_FELCA
AccessioniPrimary (citable) accession number: Q9MYW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: January 23, 2007
Last modified: April 13, 2016
This is version 80 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.