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Q9MYW6

- XDH_FELCA

UniProt

Q9MYW6 - XDH_FELCA

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Protein

Xanthine dehydrogenase/oxidase

Gene

XDH

Organism
Felis catus (Cat) (Felis silvestris catus)
Status
Reviewed - 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).By similarity

Catalytic activityi

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

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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi43 – 431Iron-sulfur 1By similarity
Metal bindingi48 – 481Iron-sulfur 1By similarity
Metal bindingi51 – 511Iron-sulfur 1By similarity
Metal bindingi73 – 731Iron-sulfur 1By similarity
Metal bindingi113 – 1131Iron-sulfur 2By similarity
Metal bindingi116 – 1161Iron-sulfur 2By similarity
Metal bindingi148 – 1481Iron-sulfur 2By similarity
Metal bindingi150 – 1501Iron-sulfur 2By similarity
Binding sitei335 – 3351FADBy similarity
Binding sitei358 – 3581FADBy similarity
Binding sitei402 – 4021FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei420 – 4201FADBy similarity
Metal bindingi766 – 7661MolybdenumBy similarity
Metal bindingi797 – 7971Molybdenum; via carbonyl oxygenBy similarity
Binding sitei801 – 8011SubstrateBy similarity
Binding sitei879 – 8791SubstrateBy similarity
Metal bindingi911 – 9111Molybdenum; via amide nitrogenBy similarity
Binding sitei913 – 9131SubstrateBy similarity
Binding sitei1009 – 10091Substrate; via amide nitrogenBy similarity
Metal bindingi1078 – 10781Molybdenum; via amide nitrogenBy similarity
Active sitei1260 – 12601Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi257 – 2648FADBy similarity
Nucleotide bindingi345 – 3495FADBy similarity

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB
  2. electron carrier activity Source: InterPro
  3. flavin adenine dinucleotide binding Source: UniProtKB
  4. iron ion binding Source: InterPro
  5. molybdopterin cofactor binding Source: UniProtKB
  6. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro
  7. xanthine dehydrogenase activity Source: UniProtKB
  8. xanthine oxidase activity Source: UniProtKB

GO - Biological processi

  1. xanthine catabolic process Source: UniProtKB
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:1.17.1.4)
Short name:
XD
Xanthine oxidase (EC:1.17.3.2)
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
ProteomesiUP000011712: Unplaced

Subcellular locationi

Cytoplasm By similarity. Peroxisome By similarity. Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
  2. peroxisome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 13311330Xanthine dehydrogenase/oxidasePRO_0000246176Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi534 ↔ 991In oxidase formBy similarity
Glycosylationi1072 – 10721N-linked (GlcNAc...)Sequence Analysis

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

Structurei

3D structure databases

ProteinModelPortaliQ9MYW6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 91882Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini229 – 412184FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

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

eggNOGiCOG4630.
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 .
RefSeqi NP_001009217.1. NM_001009217.1.

3D structure databases

ProteinModelPortali Q9MYW6.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 493692.
KEGGi fca:493692.

Organism-specific databases

CTDi 7498.

Phylogenomic databases

eggNOGi COG4630.
HOVERGENi HBG004182.
InParanoidi Q9MYW6.
KOi K00106.

Family and domain databases

Gene3Di 1.10.150.120. 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.
InterProi IPR002888. 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 ]
Pfami 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 ]
PIRSFi PIRSF000127. Xanthine_DH. 1 hit.
SMARTi SM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view ]
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.
TIGRFAMsi TIGR02963. xanthine_xdhA. 1 hit.
PROSITEi PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning of a cDNA coding for feline liver xanthine dehydrogenase."
    Tsuchida S., Yamada R., Ikemoto S., Tagawa M.
    J. Vet. Med. Sci. 63:353-355(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.

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: November 26, 2014
This is version 74 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

External Data

Dasty 3