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Q9MYW6 (XDH_FELCA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismFelis catus (Cat) (Felis silvestris catus) [Complete proteome]
Taxonomic identifier9685 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Feliformia › Felidae › Felinae › Felis

Protein attributes

Sequence length1331 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

Xanthine + NAD+ + H2O = urate + NADH.

Hypoxanthine + NAD+ + H2O = xanthine + NADH.

Xanthine + H2O + O2 = urate + H2O2.

Cofactor

Binds 2 2Fe-2S clusters By similarity.

FAD By similarity.

Binds 1 molybdenum ion (molybdopterin) per subunit By similarity.

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 By similarity.

Post-translational modification

Subject to partial proteolysis By similarity; 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.

Sequence similarities

Belongs to the xanthine dehydrogenase family.

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

Contains 1 FAD-binding PCMH-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 13311330Xanthine dehydrogenase/oxidase
PRO_0000246176

Regions

Domain4 – 91882Fe-2S ferredoxin-type
Domain229 – 412184FAD-binding PCMH-type
Nucleotide binding257 – 2648FAD By similarity
Nucleotide binding345 – 3495FAD By similarity

Sites

Active site12601Proton acceptor By similarity
Metal binding431Iron-sulfur 1 By similarity
Metal binding481Iron-sulfur 1 By similarity
Metal binding511Iron-sulfur 1 By similarity
Metal binding731Iron-sulfur 1 By similarity
Metal binding1131Iron-sulfur 2 By similarity
Metal binding1161Iron-sulfur 2 By similarity
Metal binding1481Iron-sulfur 2 By similarity
Metal binding1501Iron-sulfur 2 By similarity
Metal binding7661Molybdenum By similarity
Metal binding7971Molybdenum; via carbonyl oxygen By similarity
Metal binding9111Molybdenum; via amide nitrogen By similarity
Metal binding10781Molybdenum; via amide nitrogen By similarity
Binding site3351FAD By similarity
Binding site3581FAD By similarity
Binding site4021FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site4201FAD By similarity
Binding site8011Substrate By similarity
Binding site8791Substrate By similarity
Binding site9131Substrate By similarity
Binding site10091Substrate; via amide nitrogen By similarity

Amino acid modifications

Glycosylation10721N-linked (GlcNAc...) Potential
Disulfide bond534 ↔ 991In oxidase form By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9MYW6 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 726C4F72C3B5FB09

FASTA1,331146,122
        10         20         30         40         50         60 
MTADELVFFV NGKKVVEKNA DPETTLLAYL RRKLGLSGTK LGCGEGGCGA CTVMLSKYDR 

        70         80         90        100        110        120 
FQNKIVHFSA NACLAPICSL HHVAVTTVEG IGSTKSRLHP VQERIAKSHG SQCGFCTPGI 

       130        140        150        160        170        180 
VMSMYTLLRN QPEPTIEEIE DAFQGNLCRC TGYRPILQGF RTFARDGGCC GGSGNDLNCC 

       190        200        210        220        230        240 
MNQKTDHKIT LSPSLFNPEE FTPLDPTQEP IFPPELLRLK DTPQKQLRFE GERVTWIQAS 

       250        260        270        280        290        300 
TLQELLDLKA QDPEAKLVVG NTEIGIEMKF KNMLFPKMVC PAWIPEPVEH GPEGISFGAS 

       310        320        330        340        350        360 
CPLSLVEKTL LDAVANLPAH QTEVFKGVLE QLRWFAGKQV KSVASIGGNI ITASPISDLN 

       370        380        390        400        410        420 
PVFMASGAKL TIVSTGTRRT VRMDHTFFPA YRKTLLAPEE ILLSIEIPYS REGEYFSAFK 

       430        440        450        460        470        480 
QASRREDDIA KVTSGMRVLF NPGTAQVKEL ALCYGGMHDR TVSALQTTRK QISNFWNEEL 

       490        500        510        520        530        540 
LQNVCAGLAE ELSLAPDAPG GMVEFRRTLT LSFFFKFYLT VLQKLGIQNS KDKCGKLDPT 

       550        560        570        580        590        600 
HASATLLFQK DPPANVQLFQ EVPKGQCEED MVGRPLPHLA AAMQASGEAV YCDDIPRYEN 

       610        620        630        640        650        660 
ELSLRLVTST RAHAKIKSID TSEAQKVPGF VCFISADDVP GSNITGIGND EMVFAKDKVT 

       670        680        690        700        710        720 
CIGHIIGAVV TDTREHAQRA AQAVRITYED LPAIITIEDA IAKDSFYEPE LKIEKGNLTK 

       730        740        750        760        770        780 
GFSEADNIVS GELYIGGQEH FYLETHCTIA VPKGEAGEME LFVSTQNTTK TQSFVANMLG 

       790        800        810        820        830        840 
VPANRILVRV KRMGGGFGGK ETRSTVVSTA VPLAAYKTGR PVRCMLDRDE DMLITGGRHP 

       850        860        870        880        890        900 
FLARYKVGFM KTGRVVALKV EHYSNAGNTL DLSQSIMERA LFHMDNCYNI PNIRGTGRIC 

       910        920        930        940        950        960 
KTNLPSNTAF RGFGGPQGML IAEHWMSEVA VTCGLPAEEV RRKNMYKEGD LTHFNQKLEG 

       970        980        990       1000       1010       1020 
FTLPRCWEEC LASSQYHARK READKFNEEN CWKKRGLSII PTKFGISFTV PFLNQAGALV 

      1030       1040       1050       1060       1070       1080 
HVYTDGSVLL THGGTEMGQG LHTKMVQVAS RALKIPTSKI YISETSTNTV PNTSPTAASV 

      1090       1100       1110       1120       1130       1140 
STDINGQAVY EACQTILKRL EPFKKKNPSG SWEDWVTAAY LDAVSLSATG FYKTPNIGYS 

      1150       1160       1170       1180       1190       1200 
FETNSGNPFH YFSYGVACSE VEIDCLTGDH KNLRTDIVMD VGSSLNPAID IGQVEGAFVQ 

      1210       1220       1230       1240       1250       1260 
GLGLFTLEEL HYSPEGSLHT RGPSTYKIPA FGSIPSEFRV SLLRDCPNKK AIYASKAVGE 

      1270       1280       1290       1300       1310       1320 
PPLFLAASIF FAIKDAICAA RAGNPDCKTK KLFQLNSPAT PEKIRNACVD QFTRLCVTGT 

      1330 
AESCKPWSVR V

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References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF286379 mRNA. Translation: AAF97949.1.
RefSeqNP_001009217.1. NM_001009217.1.

3D structure databases

ProteinModelPortalQ9MYW6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID493692.
KEGGfca:493692.

Organism-specific databases

CTD7498.

Phylogenomic databases

eggNOGCOG4630.
HOVERGENHBG004182.
KOK00106.

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. 2Fe-2S_bind. 1 hit.
SSF56003. Ald_xan_DH_mo_bd. 1 hit.
SSF54665. Aldxan_dh_hamm. 1 hit.
SSF55447. CO_deh_flav_C. 1 hit.
SSF56176. FAD-binding_2. 1 hit.
SSF54292. Ferredoxin. 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...

Entry information

Entry nameXDH_FELCA
AccessionPrimary (citable) accession number: Q9MYW6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 69 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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