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Q9MYW6

- XDH_FELCA

UniProt

Q9MYW6 - XDH_FELCA

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
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    Binds 2 2Fe-2S clusters.By similarity
    FAD.By similarity
    Binds 1 molybdenum-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

    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-SubCell
    2. peroxisome Source: UniProtKB-SubCell

    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.
    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

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    MTADELVFFV NGKKVVEKNA DPETTLLAYL RRKLGLSGTK LGCGEGGCGA     50
    CTVMLSKYDR FQNKIVHFSA NACLAPICSL HHVAVTTVEG IGSTKSRLHP 100
    VQERIAKSHG SQCGFCTPGI VMSMYTLLRN QPEPTIEEIE DAFQGNLCRC 150
    TGYRPILQGF RTFARDGGCC GGSGNDLNCC MNQKTDHKIT LSPSLFNPEE 200
    FTPLDPTQEP IFPPELLRLK DTPQKQLRFE GERVTWIQAS TLQELLDLKA 250
    QDPEAKLVVG NTEIGIEMKF KNMLFPKMVC PAWIPEPVEH GPEGISFGAS 300
    CPLSLVEKTL LDAVANLPAH QTEVFKGVLE QLRWFAGKQV KSVASIGGNI 350
    ITASPISDLN PVFMASGAKL TIVSTGTRRT VRMDHTFFPA YRKTLLAPEE 400
    ILLSIEIPYS REGEYFSAFK QASRREDDIA KVTSGMRVLF NPGTAQVKEL 450
    ALCYGGMHDR TVSALQTTRK QISNFWNEEL LQNVCAGLAE ELSLAPDAPG 500
    GMVEFRRTLT LSFFFKFYLT VLQKLGIQNS KDKCGKLDPT HASATLLFQK 550
    DPPANVQLFQ EVPKGQCEED MVGRPLPHLA AAMQASGEAV YCDDIPRYEN 600
    ELSLRLVTST RAHAKIKSID TSEAQKVPGF VCFISADDVP GSNITGIGND 650
    EMVFAKDKVT CIGHIIGAVV TDTREHAQRA AQAVRITYED LPAIITIEDA 700
    IAKDSFYEPE LKIEKGNLTK GFSEADNIVS GELYIGGQEH FYLETHCTIA 750
    VPKGEAGEME LFVSTQNTTK TQSFVANMLG VPANRILVRV KRMGGGFGGK 800
    ETRSTVVSTA VPLAAYKTGR PVRCMLDRDE DMLITGGRHP FLARYKVGFM 850
    KTGRVVALKV EHYSNAGNTL DLSQSIMERA LFHMDNCYNI PNIRGTGRIC 900
    KTNLPSNTAF RGFGGPQGML IAEHWMSEVA VTCGLPAEEV RRKNMYKEGD 950
    LTHFNQKLEG FTLPRCWEEC LASSQYHARK READKFNEEN CWKKRGLSII 1000
    PTKFGISFTV PFLNQAGALV HVYTDGSVLL THGGTEMGQG LHTKMVQVAS 1050
    RALKIPTSKI YISETSTNTV PNTSPTAASV STDINGQAVY EACQTILKRL 1100
    EPFKKKNPSG SWEDWVTAAY LDAVSLSATG FYKTPNIGYS FETNSGNPFH 1150
    YFSYGVACSE VEIDCLTGDH KNLRTDIVMD VGSSLNPAID IGQVEGAFVQ 1200
    GLGLFTLEEL HYSPEGSLHT RGPSTYKIPA FGSIPSEFRV SLLRDCPNKK 1250
    AIYASKAVGE PPLFLAASIF FAIKDAICAA RAGNPDCKTK KLFQLNSPAT 1300
    PEKIRNACVD QFTRLCVTGT AESCKPWSVR V 1331
    Length:1,331
    Mass (Da):146,122
    Last modified:January 23, 2007 - v3
    Checksum:i726C4F72C3B5FB09
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.
    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: October 1, 2014
    This is version 72 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