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P22985

- XDH_RAT

UniProt

P22985 - XDH_RAT

Protein

Xanthine dehydrogenase/oxidase

Gene

Xdh

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (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.1 Publication

    Catalytic activityi

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

    Cofactori

    Binds 2 2Fe-2S clusters.
    FAD.
    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.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi43 – 431Iron-sulfur 1
    Metal bindingi48 – 481Iron-sulfur 1
    Metal bindingi51 – 511Iron-sulfur 1
    Metal bindingi73 – 731Iron-sulfur 1
    Metal bindingi112 – 1121Iron-sulfur 2
    Metal bindingi115 – 1151Iron-sulfur 2
    Metal bindingi147 – 1471Iron-sulfur 2
    Metal bindingi149 – 1491Iron-sulfur 2
    Binding sitei336 – 3361FADBy similarity
    Binding sitei359 – 3591FAD2 Publications
    Binding sitei403 – 4031FAD; via amide nitrogen and carbonyl oxygen2 Publications
    Binding sitei421 – 4211FADBy similarity
    Metal bindingi767 – 7671MolybdenumBy similarity
    Metal bindingi798 – 7981Molybdenum; via carbonyl oxygenBy similarity
    Binding sitei802 – 8021Substrate
    Binding sitei880 – 8801Substrate
    Metal bindingi912 – 9121Molybdenum; via amide nitrogenBy similarity
    Binding sitei914 – 9141SubstrateBy similarity
    Binding sitei1010 – 10101Substrate; via amide nitrogen
    Metal bindingi1079 – 10791Molybdenum; via amide nitrogenBy similarity
    Active sitei1261 – 12611Proton acceptor

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi256 – 2638FAD2 Publications
    Nucleotide bindingi346 – 3505FAD2 Publications

    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. bone resorption Source: RGD
    2. response to aluminum ion Source: RGD
    3. xanthine catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15163.

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi62043. Xdh.

    Subcellular locationi

    Peroxisome 1 Publication. Cytoplasm 1 Publication. Secreted By similarity

    GO - Cellular componenti

    1. cytosol Source: RGD
    2. extracellular space Source: RGD
    3. peroxisome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Peroxisome, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi335 – 3362WF → AL: Converts the enzyme to the oxidase form that utilizes molecular oxygen as electron acceptor. Interferes with normal conversion to the dehydrogenase form by reducing agents. 1 Publication
    Mutagenesisi535 – 5351C → A: Slows the conversion from the dehydrogenase form to the oxidase form; when associated with R-992. Abolishes conversion from the dehydrogenase form to the oxidase form; when associated with R-992 and S-1316. 2 Publications
    Mutagenesisi992 – 9921C → R: Slows the conversion from the dehydrogenase form to the oxidase form; when associated with A-535. Abolishes conversion from the dehydrogenase form to the oxidase form; when associated with A-535 and S-1316. 2 Publications
    Mutagenesisi1316 – 13161C → S: Abolishes conversion from the dehydrogenase form to the oxidase form; when associated with A-535 and R-992. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 13311330Xanthine dehydrogenase/oxidasePRO_0000166086Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi535 ↔ 992In oxidase form1 Publication
    Glycosylationi1073 – 10731N-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).
    Contains sulfhydryl groups that are easily oxidized (in vitro); this alters the enzyme from the dehydrogenase form (D) to the oxidase form (O).

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP22985.
    PRIDEiP22985.

    Expressioni

    Inductioni

    By interferon.

    Gene expression databases

    GenevestigatoriP22985.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with BTN1A1 By similarity.By similarity

    Structurei

    Secondary structure

    1
    1331
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 105
    Beta strandi13 – 175
    Helixi26 – 327
    Beta strandi44 – 485
    Beta strandi52 – 598
    Turni60 – 634
    Beta strandi64 – 718
    Helixi72 – 743
    Helixi77 – 793
    Beta strandi84 – 863
    Helixi88 – 914
    Beta strandi94 – 963
    Helixi99 – 1068
    Helixi116 – 12914
    Helixi135 – 1406
    Turni141 – 1444
    Beta strandi148 – 1503
    Helixi153 – 1597
    Helixi160 – 1623
    Helixi197 – 1993
    Helixi205 – 2073
    Helixi213 – 2186
    Beta strandi226 – 2294
    Beta strandi234 – 2374
    Helixi241 – 25010
    Helixi263 – 2697
    Beta strandi275 – 2795
    Helixi284 – 2874
    Beta strandi289 – 2913
    Beta strandi293 – 2997
    Helixi304 – 31714
    Helixi320 – 3223
    Helixi324 – 33411
    Helixi339 – 3424
    Helixi347 – 3537
    Helixi361 – 3666
    Beta strandi370 – 3756
    Beta strandi378 – 3836
    Helixi386 – 3883
    Beta strandi402 – 4098
    Beta strandi415 – 4228
    Beta strandi424 – 4285
    Beta strandi432 – 44110
    Beta strandi445 – 46117
    Turni466 – 4683
    Helixi470 – 4723
    Beta strandi476 – 4783
    Helixi479 – 49214
    Helixi504 – 52825
    Helixi532 – 5354
    Helixi540 – 5467
    Beta strandi555 – 5595
    Beta strandi565 – 5673
    Helixi582 – 5865
    Helixi593 – 5953
    Beta strandi603 – 6097
    Beta strandi611 – 62111
    Helixi625 – 6273
    Beta strandi631 – 6355
    Helixi637 – 6393
    Beta strandi645 – 6473
    Beta strandi652 – 6554
    Beta strandi658 – 6603
    Beta strandi666 – 6749
    Helixi675 – 6839
    Beta strandi686 – 6916
    Helixi698 – 7036
    Beta strandi707 – 7104
    Beta strandi712 – 7176
    Helixi719 – 7257
    Beta strandi727 – 73610
    Beta strandi748 – 7536
    Beta strandi760 – 7645
    Helixi769 – 78012
    Helixi784 – 7863
    Beta strandi787 – 7926
    Turni798 – 8014
    Beta strandi802 – 8043
    Helixi806 – 81914
    Beta strandi823 – 8264
    Helixi829 – 8357
    Beta strandi842 – 8509
    Beta strandi856 – 86611
    Helixi874 – 88310
    Turni884 – 8885
    Beta strandi892 – 90110
    Turni912 – 9154
    Helixi916 – 93419
    Helixi938 – 9458
    Helixi964 – 97411
    Helixi977 – 99014
    Beta strandi992 – 100817
    Helixi1012 – 10143
    Beta strandi1016 – 10238
    Beta strandi1029 – 10346
    Beta strandi1038 – 10403
    Helixi1042 – 105413
    Helixi1058 – 10603
    Beta strandi1061 – 10633
    Turni1068 – 10703
    Turni1079 – 10813
    Helixi1082 – 110726
    Beta strandi1108 – 11114
    Helixi1113 – 112210
    Beta strandi1128 – 11347
    Turni1142 – 11454
    Beta strandi1151 – 116515
    Turni1166 – 11683
    Beta strandi1171 – 118111
    Helixi1188 – 120720
    Turni1224 – 12263
    Helixi1232 – 12343
    Beta strandi1237 – 12437
    Turni1250 – 12523
    Helixi1253 – 12553
    Helixi1264 – 12674
    Helixi1268 – 128518
    Beta strandi1286 – 12894
    Helixi1301 – 13077
    Helixi1311 – 13166

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WYGX-ray2.60A1-1331[»]
    2E3TX-ray2.28A/B1-1331[»]
    3AN1X-ray1.73A/B1-1331[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22985.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 91882Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini228 – 413186FAD-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.
    HOGENOMiHOG000191197.
    HOVERGENiHBG004182.
    InParanoidiP22985.
    KOiK00106.
    PhylomeDBiP22985.

    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.

    P22985-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTADELVFFV NGKKVVEKNA DPETTLLVYL RRKLGLCGTK LGCGEGGCGA     50
    CTVMISKYDR LQNKIVHFSV NACLAPICSL HHVAVTTVEG IGNTQKLHPV 100
    QERIARSHGS QCGFCTPGIV MSMYTLLRNQ PEPTVEEIEN AFQGNLCRCT 150
    GYRPILQGFR TFAKDGGCCG GSGNNPNCCM NQTKDQTVSL SPSLFNPEDF 200
    KPLDPTQEPI FPPELLRLKD TPQKKLRFEG ERVTWIQAST MEELLDLKAQ 250
    HPDAKLVVGN TEIGIEMKFK NMLFPLIVCP AWIPELNSVV HGPEGISFGA 300
    SCPLSLVESV LAEEIAKLPE QKTEVFRGVM EQLRWFAGKQ VKSVASIGGN 350
    IITASPISDL NPVFMASGAK LTLVSRGTRR TVRMDHTFFP GYRKTLLRPE 400
    EILLSIEIPY SKEGEFFSAF KQASRREDDI AKVTSGMRVL FKPGTIEVQE 450
    LSLCFGGMAD RTISALKTTP KQLSKSWNEE LLQSVCAGLA EELQLAPDAP 500
    GGMVEFRRTL TLSFFFKFYL TVLQKLGRAD LEDMCGKLDP TFASATLLFQ 550
    KDPPANVQLF QEVPKDQSEE DMVGRPLPHL AANMQASGEA VYCDDIPRYE 600
    NELSLRLVTS TRAHAKITSI DTSEAKKVPG FVCFLTAEDV PNSNATGLFN 650
    DETVFAKDEV TCVGHIIGAV VADTPEHAQR AARGVKITYE DLPAIITIQD 700
    AINNNSFYGS EIKIEKGDLK KGFSEADNVV SGELYIGGQE HFYLETNCTI 750
    AVPKGEAGEM ELFVSTQNTM KTQSFVAKML GVPDNRIVVR VKRMGGGFGG 800
    KETRSTVVST ALALAAHKTG RPVRCMLDRD EDMLITGGRH PFLAKYKVGF 850
    MKTGTVVALE VAHFSNGGNT EDLSRSIMER ALFHMDNAYK IPNIRGTGRI 900
    CKTNLPSNTA FRGFGGPQGM LIAEYWMSEV AITCGLPAEE VRRKNMYKEG 950
    DLTHFNQKLE GFTLPRCWDE CIASSQYLAR KREVEKFNRE NCWKKRGLCI 1000
    IPTKFGISFT LPFLNQGGAL VHVYTDGSVL LTHGGTEMGQ GLHTKMVQVA 1050
    SRALKIPTSK IHISETSTNT VPNTSPTAAS ASADLNGQGV YEACQTILKR 1100
    LEPFKKKKPT GPWEAWVMDA YTSAVSLSAT GFYKTPNLGY SFETNSGNPF 1150
    HYFSYGVACS EVEIDCLTGD HKNLRTDIVM DVGSSLNPAI DIGQVEGAFV 1200
    QGLGLFTMEE LHYSPEGSLH TRGPSTYKIP AFGSIPIEFR VSLLRDCPNK 1250
    RAIYASKAVG EPPLFLASSI FFAIKDAIRA ARAQHGDNAK QLFQLDSPAT 1300
    PEKIRNACVD QFTTLCVTGV PENCKSWSVR I 1331
    Length:1,331
    Mass (Da):146,243
    Last modified:January 23, 2007 - v3
    Checksum:iBF2586A9C63A0B2C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05579 mRNA. Translation: AAA42349.1.
    AH000836 Unassigned DNA. Translation: AAA18869.1.
    RefSeqiNP_058850.1. NM_017154.1.
    UniGeneiRn.202951.

    Genome annotation databases

    GeneIDi497811.
    KEGGirno:497811.
    UCSCiRGD:62043. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05579 mRNA. Translation: AAA42349.1 .
    AH000836 Unassigned DNA. Translation: AAA18869.1 .
    RefSeqi NP_058850.1. NM_017154.1.
    UniGenei Rn.202951.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WYG X-ray 2.60 A 1-1331 [» ]
    2E3T X-ray 2.28 A/B 1-1331 [» ]
    3AN1 X-ray 1.73 A/B 1-1331 [» ]
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P22985.
    ChEMBLi CHEMBL1075246.

    Proteomic databases

    PaxDbi P22985.
    PRIDEi P22985.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 497811.
    KEGGi rno:497811.
    UCSCi RGD:62043. rat.

    Organism-specific databases

    CTDi 7498.
    RGDi 62043. Xdh.

    Phylogenomic databases

    eggNOGi COG4630.
    HOGENOMi HOG000191197.
    HOVERGENi HBG004182.
    InParanoidi P22985.
    KOi K00106.
    PhylomeDBi P22985.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-15163.

    Miscellaneous databases

    EvolutionaryTracei P22985.
    NextBioi 697781.
    PROi P22985.

    Gene expression databases

    Genevestigatori P22985.

    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. "Proteolytic conversion of xanthine dehydrogenase from the NAD-dependent type to the O2-dependent type. Amino acid sequence of rat liver xanthine dehydrogenase and identification of the cleavage sites of the enzyme protein during irreversible conversion by trypsin."
      Amaya Y., Yamazaki K., Sato M., Noda K., Nishino T., Nishino T.
      J. Biol. Chem. 265:14170-14175(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ENZYME REGULATION, PROTEOLYTIC CONVERSION, SUBUNIT.
      Tissue: Liver.
    2. "Identification of the rat xanthine dehydrogenase/oxidase promoter."
      Chow C.W., Clark M., Rinaldo J., Chalkley R.
      Nucleic Acids Res. 22:1846-1854(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 1-55.
      Strain: Sprague-Dawley.
    3. "Ultrastructural localization of xanthine oxidoreductase activity in isolated rat liver cells."
      Frederiks W.M., Vreeling-Sindelarova H.
      Acta Histochem. 104:29-37(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    4. "Mechanism of the conversion of xanthine dehydrogenase to xanthine oxidase: identification of the two cysteine disulfide bonds and crystal structure of a non-convertible rat liver xanthine dehydrogenase mutant."
      Nishino T., Okamoto K., Kawaguchi Y., Hori H., Matsumura T., Eger B.T., Pai E.F., Nishino T.
      J. Biol. Chem. 280:24888-24894(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF MUTANT ALA-535/ARG-992/SER-1324 IN COMPLEX WITH FAD; URIC ACID AND IRON-SULFUR CENTERS, CATALYTIC ACTIVITY, DISULFIDE BOND, ENZYME REGULATION, MUTAGENESIS OF CYS-535; CYS-992 AND CYS-1316, COFACTOR.
    5. "Two mutations convert mammalian xanthine oxidoreductase to highly superoxide-productive xanthine oxidase."
      Asai R., Nishino T., Matsumura T., Okamoto K., Igarashi K., Pai E.F., Nishino T.
      J. Biochem. 141:525-534(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF MUTANT ALA-335/LEU-336 IN COMPLEX WITH FAD AND IRON-SULFUR CENTER, MUTAGENESIS OF 335-TRP-PHE-336, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.

    Entry informationi

    Entry nameiXDH_RAT
    AccessioniPrimary (citable) accession number: P22985
    Secondary accession number(s): Q63157
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 136 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3