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P80457

- XDH_BOVIN

UniProt

P80457 - XDH_BOVIN

Protein

Xanthine dehydrogenase/oxidase

Gene

XDH

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 4 (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.

    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.

    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.3 Publications

    Kineticsi

    1. KM=111 µM for molecular oxygen in dehydrogenase form2 Publications
    2. KM=37.7 µM for molecular oxygen in oxygenase form2 Publications
    3. KM=20.8 µM for NAD2 Publications
    4. KM=5 µM for xanthine2 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 bindingi113 – 1131Iron-sulfur 2
    Metal bindingi116 – 1161Iron-sulfur 2
    Metal bindingi148 – 1481Iron-sulfur 2
    Metal bindingi150 – 1501Iron-sulfur 2
    Binding sitei337 – 3371FAD2 Publications
    Binding sitei360 – 3601FAD2 Publications
    Binding sitei404 – 4041FAD; via amide nitrogen and carbonyl oxygen2 Publications
    Binding sitei422 – 4221FAD2 Publications
    Metal bindingi767 – 7671Molybdenum
    Metal bindingi798 – 7981Molybdenum; via carbonyl oxygen
    Binding sitei802 – 8021Substrate
    Binding sitei880 – 8801Substrate
    Metal bindingi912 – 9121Molybdenum; via amide nitrogen
    Binding sitei914 – 9141Substrate
    Binding sitei1010 – 10101Substrate; via amide nitrogen
    Metal bindingi1079 – 10791Molybdenum; via amide nitrogen
    Active sitei1261 – 12611Proton acceptor1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi257 – 2648FAD2 Publications
    Nucleotide bindingi347 – 3515FAD2 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. 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

    SABIO-RKP80457.

    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
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    Cytoplasm By similarity. Peroxisome. Secreted

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. peroxisome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Peroxisome, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi335 – 3351R → A: Promotes conversion to the oxidase form that utilizes molecular oxygen as electron acceptor. Interferes with normal conversion to the dehydrogenase form by reducing agents. 1 Publication
    Mutagenesisi336 – 3361W → A: Promotes conversion to the oxidase form that utilizes molecular oxygen as electron acceptor. Interferes with normal conversion to the dehydrogenase form by reducing agents. 1 Publication
    Mutagenesisi427 – 4271R → Q: Promotes conversion to the oxidase form that utilizes molecular oxygen as electron acceptor. Interferes with normal conversion to the dehydrogenase form by reducing agents. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 13321331Xanthine dehydrogenase/oxidasePRO_0000166082Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi535 ↔ 992In oxidase formBy similarity
    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

    PaxDbiP80457.
    PRIDEiP80457.

    Expressioni

    Tissue specificityi

    Detected in milk (at protein level).3 Publications

    Interactioni

    Subunit structurei

    Homodimer. Interacts with BTN1A1 By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000032520.

    Structurei

    Secondary structure

    1
    1332
    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
    Turni72 – 743
    Helixi77 – 793
    Beta strandi84 – 863
    Helixi88 – 903
    Beta strandi94 – 963
    Helixi100 – 1078
    Helixi117 – 13014
    Helixi136 – 1405
    Turni142 – 1454
    Beta strandi149 – 1513
    Helixi154 – 1618
    Helixi198 – 2003
    Helixi206 – 2083
    Helixi214 – 2185
    Helixi219 – 2213
    Beta strandi227 – 2304
    Beta strandi235 – 2384
    Helixi242 – 25110
    Helixi264 – 2707
    Beta strandi276 – 2805
    Helixi285 – 2873
    Beta strandi290 – 2923
    Beta strandi294 – 3007
    Helixi305 – 31814
    Helixi321 – 3233
    Helixi325 – 33410
    Beta strandi336 – 3383
    Helixi340 – 3434
    Helixi348 – 3547
    Helixi362 – 3676
    Beta strandi371 – 3766
    Beta strandi379 – 3846
    Helixi387 – 3893
    Beta strandi403 – 4108
    Beta strandi416 – 4227
    Beta strandi428 – 4314
    Beta strandi435 – 4439
    Beta strandi446 – 46217
    Helixi467 – 4715
    Turni472 – 4754
    Beta strandi477 – 4793
    Helixi480 – 49314
    Helixi505 – 52723
    Turni540 – 5423
    Helixi543 – 5464
    Beta strandi555 – 5595
    Helixi582 – 5865
    Helixi593 – 5953
    Beta strandi603 – 6097
    Beta strandi611 – 62111
    Helixi625 – 6273
    Beta strandi631 – 6355
    Helixi637 – 6393
    Beta strandi644 – 6474
    Beta strandi652 – 6554
    Beta strandi658 – 6603
    Beta strandi666 – 6749
    Helixi675 – 6839
    Beta strandi686 – 6916
    Helixi698 – 7036
    Beta strandi707 – 71711
    Helixi719 – 7257
    Beta strandi727 – 73610
    Beta strandi748 – 7536
    Beta strandi760 – 7645
    Helixi769 – 78012
    Helixi784 – 7863
    Beta strandi787 – 7915
    Turni798 – 8014
    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
    Helixi1113 – 112210
    Beta strandi1128 – 11347
    Turni1142 – 11454
    Beta strandi1151 – 116515
    Turni1166 – 11683
    Beta strandi1171 – 118111
    Helixi1188 – 120720
    Turni1224 – 12263
    Helixi1232 – 12343
    Beta strandi1237 – 12437
    Helixi1253 – 12553
    Helixi1264 – 12674
    Helixi1268 – 128518
    Helixi1302 – 13087
    Turni1312 – 13143
    Helixi1317 – 13193

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FIQX-ray2.50A1-219[»]
    B220-569[»]
    C570-1332[»]
    1FO4X-ray2.10A/B1-1332[»]
    1N5XX-ray2.80A/B2-1332[»]
    1V97X-ray1.94A/B1-1332[»]
    1VDVX-ray1.98A/B1-1332[»]
    3AM9X-ray2.17A/B1-1332[»]
    3AMZX-ray2.10A/B1-1332[»]
    3AX7X-ray2.34A/B1-1332[»]
    3AX9X-ray2.30A/B1-1332[»]
    3B9JX-ray2.30A/I1-219[»]
    B/J220-569[»]
    C/K570-1332[»]
    3BDJX-ray2.00A/B1-1332[»]
    3ETRX-ray2.20A/L2-165[»]
    B/M224-528[»]
    C/N571-1325[»]
    3EUBX-ray2.602/A/J/S1-165[»]
    3/B/K/T224-528[»]
    4/C/L/U571-1332[»]
    3NRZX-ray1.80A/J2-165[»]
    B/K224-528[»]
    C/L571-1326[»]
    3NS1X-ray2.60A/J2-165[»]
    B/K224-528[»]
    C/L571-1325[»]
    3NVVX-ray1.82A/J2-165[»]
    B/K195-528[»]
    C/L571-1325[»]
    3NVWX-ray1.60A/J2-165[»]
    B/K195-528[»]
    C/L571-1326[»]
    3NVYX-ray2.00A/J2-165[»]
    B/K195-528[»]
    C/L571-1326[»]
    3NVZX-ray1.60A/J2-165[»]
    B/K224-528[»]
    C/L571-1325[»]
    3SR6X-ray2.10A/J2-165[»]
    B/K224-528[»]
    C/L571-1315[»]
    3UNAX-ray1.90A/B1-1332[»]
    3UNCX-ray1.65A/B1-1332[»]
    3UNIX-ray2.20A/B1-1332[»]
    DisProtiDP00450.
    ProteinModelPortaliP80457.
    SMRiP80457. Positions 2-165, 224-528, 571-1328.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP80457.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 91882Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini229 – 414186FAD-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.
    InParanoidiP80457.
    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.

    P80457-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTADELVFFV NGKKVVEKNA DPETTLLAYL RRKLGLRGTK LGCGEGGCGA     50
    CTVMLSKYDR LQDKIIHFSA NACLAPICTL HHVAVTTVEG IGSTKTRLHP 100
    VQERIAKSHG SQCGFCTPGI VMSMYTLLRN QPEPTVEEIE DAFQGNLCRC 150
    TGYRPILQGF RTFAKNGGCC GGNGNNPNCC MNQKKDHTVT LSPSLFNPEE 200
    FMPLDPTQEP IFPPELLRLK DVPPKQLRFE GERVTWIQAS TLKELLDLKA 250
    QHPEAKLVVG NTEIGIEMKF KNQLFPMIIC PAWIPELNAV EHGPEGISFG 300
    AACALSSVEK TLLEAVAKLP TQKTEVFRGV LEQLRWFAGK QVKSVASLGG 350
    NIITASPISD LNPVFMASGT KLTIVSRGTR RTVPMDHTFF PSYRKTLLGP 400
    EEILLSIEIP YSREDEFFSA FKQASRREDD IAKVTCGMRV LFQPGSMQVK 450
    ELALCYGGMA DRTISALKTT QKQLSKFWNE KLLQDVCAGL AEELSLSPDA 500
    PGGMIEFRRT LTLSFFFKFY LTVLKKLGKD SKDKCGKLDP TYTSATLLFQ 550
    KDPPANIQLF QEVPNGQSKE DTVGRPLPHL AAAMQASGEA VYCDDIPRYE 600
    NELFLRLVTS TRAHAKIKSI DVSEAQKVPG FVCFLSADDI PGSNETGLFN 650
    DETVFAKDTV TCVGHIIGAV VADTPEHAER AAHVVKVTYE DLPAIITIED 700
    AIKNNSFYGS ELKIEKGDLK KGFSEADNVV SGELYIGGQD HFYLETHCTI 750
    AIPKGEEGEM ELFVSTQNAM KTQSFVAKML GVPVNRILVR VKRMGGGFGG 800
    KETRSTLVSV AVALAAYKTG HPVRCMLDRN EDMLITGGRH PFLARYKVGF 850
    MKTGTIVALE VDHYSNAGNS RDLSHSIMER ALFHMDNCYK IPNIRGTGRL 900
    CKTNLSSNTA FRGFGGPQAL FIAENWMSEV AVTCGLPAEE VRWKNMYKEG 950
    DLTHFNQRLE GFSVPRCWDE CLKSSQYYAR KSEVDKFNKE NCWKKRGLCI 1000
    IPTKFGISFT VPFLNQAGAL IHVYTDGSVL VSHGGTEMGQ GLHTKMVQVA 1050
    SKALKIPISK IYISETSTNT VPNSSPTAAS VSTDIYGQAV YEACQTILKR 1100
    LEPFKKKNPD GSWEDWVMAA YQDRVSLSTT GFYRTPNLGY SFETNSGNAF 1150
    HYFTYGVACS EVEIDCLTGD HKNLRTDIVM DVGSSLNPAI DIGQVEGAFV 1200
    QGLGLFTLEE LHYSPEGSLH TRGPSTYKIP AFGSIPTEFR VSLLRDCPNK 1250
    KAIYASKAVG EPPLFLGASV FFAIKDAIRA ARAQHTNNNT KELFRLDSPA 1300
    TPEKIRNACV DKFTTLCVTG APGNCKPWSL RV 1332
    Length:1,332
    Mass (Da):146,790
    Last modified:January 23, 2007 - v4
    Checksum:i744BA523471948B7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti188 – 1881T → TQ in CAA67117. (PubMed:9388547)Curated
    Sequence conflicti199 – 1991E → K in CAA67117. (PubMed:9388547)Curated
    Sequence conflicti366 – 3661M → V in CAA67117. (PubMed:9388547)Curated
    Sequence conflicti552 – 5521D → H in CAA58497. (PubMed:8708081)Curated
    Sequence conflicti958 – 9581R → K in CAA67117. (PubMed:9388547)Curated
    Sequence conflicti976 – 9761Q → E in CAA67117. (PubMed:9388547)Curated
    Sequence conflicti1039 – 10402GQ → E in CAA67117. (PubMed:9388547)Curated
    Sequence conflicti1244 – 12441L → V in CAA67117. (PubMed:9388547)Curated
    Sequence conflicti1268 – 12681A → P in CAA67117. (PubMed:9388547)Curated
    Sequence conflicti1279 – 12813RAA → ARG in CAA67117. (PubMed:9388547)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83508 mRNA. Translation: CAA58497.1.
    X98491 mRNA. Translation: CAA67117.1.
    PIRiS65135.
    RefSeqiNP_776397.1. NM_173972.2.
    UniGeneiBt.5403.

    Genome annotation databases

    GeneIDi280960.
    KEGGibta:280960.

    Cross-referencesi

    Web resourcesi

    Worthington enzyme manual

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83508 mRNA. Translation: CAA58497.1 .
    X98491 mRNA. Translation: CAA67117.1 .
    PIRi S65135.
    RefSeqi NP_776397.1. NM_173972.2.
    UniGenei Bt.5403.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FIQ X-ray 2.50 A 1-219 [» ]
    B 220-569 [» ]
    C 570-1332 [» ]
    1FO4 X-ray 2.10 A/B 1-1332 [» ]
    1N5X X-ray 2.80 A/B 2-1332 [» ]
    1V97 X-ray 1.94 A/B 1-1332 [» ]
    1VDV X-ray 1.98 A/B 1-1332 [» ]
    3AM9 X-ray 2.17 A/B 1-1332 [» ]
    3AMZ X-ray 2.10 A/B 1-1332 [» ]
    3AX7 X-ray 2.34 A/B 1-1332 [» ]
    3AX9 X-ray 2.30 A/B 1-1332 [» ]
    3B9J X-ray 2.30 A/I 1-219 [» ]
    B/J 220-569 [» ]
    C/K 570-1332 [» ]
    3BDJ X-ray 2.00 A/B 1-1332 [» ]
    3ETR X-ray 2.20 A/L 2-165 [» ]
    B/M 224-528 [» ]
    C/N 571-1325 [» ]
    3EUB X-ray 2.60 2/A/J/S 1-165 [» ]
    3/B/K/T 224-528 [» ]
    4/C/L/U 571-1332 [» ]
    3NRZ X-ray 1.80 A/J 2-165 [» ]
    B/K 224-528 [» ]
    C/L 571-1326 [» ]
    3NS1 X-ray 2.60 A/J 2-165 [» ]
    B/K 224-528 [» ]
    C/L 571-1325 [» ]
    3NVV X-ray 1.82 A/J 2-165 [» ]
    B/K 195-528 [» ]
    C/L 571-1325 [» ]
    3NVW X-ray 1.60 A/J 2-165 [» ]
    B/K 195-528 [» ]
    C/L 571-1326 [» ]
    3NVY X-ray 2.00 A/J 2-165 [» ]
    B/K 195-528 [» ]
    C/L 571-1326 [» ]
    3NVZ X-ray 1.60 A/J 2-165 [» ]
    B/K 224-528 [» ]
    C/L 571-1325 [» ]
    3SR6 X-ray 2.10 A/J 2-165 [» ]
    B/K 224-528 [» ]
    C/L 571-1315 [» ]
    3UNA X-ray 1.90 A/B 1-1332 [» ]
    3UNC X-ray 1.65 A/B 1-1332 [» ]
    3UNI X-ray 2.20 A/B 1-1332 [» ]
    DisProti DP00450.
    ProteinModelPortali P80457.
    SMRi P80457. Positions 2-165, 224-528, 571-1328.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000032520.

    Chemistry

    BindingDBi P80457.
    ChEMBLi CHEMBL3649.

    Proteomic databases

    PaxDbi P80457.
    PRIDEi P80457.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 280960.
    KEGGi bta:280960.

    Organism-specific databases

    CTDi 7498.

    Phylogenomic databases

    eggNOGi COG4630.
    HOGENOMi HOG000191197.
    HOVERGENi HBG004182.
    InParanoidi P80457.
    KOi K00106.

    Enzyme and pathway databases

    SABIO-RK P80457.

    Miscellaneous databases

    EvolutionaryTracei P80457.
    NextBioi 20805070.
    PROi P80457.

    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. "Purification of the bovine xanthine oxidoreductase from milk fat globule membranes and cloning of complementary deoxyribonucleic acid."
      Berglund L., Rasmussen J.T., Andersen M.D., Rasmussen M.S., Petersen T.E.
      J. Dairy Sci. 79:198-204(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Mammary gland.
    2. "The xanthine oxidoreductase gene: structure and regulation."
      Terao M., Kurosaki M., Zanotta S., Garattini E.
      Biochem. Soc. Trans. 25:791-796(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    3. "Properties of rabbit liver aldehyde oxidase and the relationship of the enzyme to xanthine oxidase and dehydrogenase."
      Turner N.A., Doyle W.A., Ventom A.M., Bray R.C.
      Eur. J. Biochem. 232:646-657(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-23; 186-205 AND 552-562.
      Tissue: Milk.
    4. "Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Purification, interconversion and some properties."
      Battelli M.G., Lorenzoni E., Stripe F.
      Biochem. J. 131:191-198(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, CONVERSION BY PARTIAL PROTEOLYSIS AND BY REDUCING AGENTS.
    5. "Unique amino acids cluster for switching from the dehydrogenase to oxidase form of xanthine oxidoreductase."
      Kuwabara Y., Nishino T., Okamoto K., Matsumura T., Eger B.T., Pai E.F., Nishino T.
      Proc. Natl. Acad. Sci. U.S.A. 100:8170-8175(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-335; TRP-336 AND ARG-427.
    6. "Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion."
      Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F.
      Proc. Natl. Acad. Sci. U.S.A. 97:10723-10728(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH FAD; IRON-SULFUR CENTERS; SALICYLATE, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    7. "An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition."
      Okamoto K., Eger B.T., Nishino T., Kondo S., Pai E.F., Nishino T.
      J. Biol. Chem. 278:1848-1855(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND SYNTHETIC INHIBITOR TEI-6720, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    8. "The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition."
      Okamoto K., Matsumoto K., Hille R., Eger B.T., Pai E.F., Nishino T.
      Proc. Natl. Acad. Sci. U.S.A. 101:7931-7936(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND INHIBITOR FYX-051, ACTIVE SITE, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    9. "Substrate orientation and catalysis at the molybdenum site in xanthine oxidase: crystal structures in complex with xanthine and lumazine."
      Pauff J.M., Cao H., Hille R.
      J. Biol. Chem. 284:8760-8767(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS; CALCIUM IONS; XANTHINE AND LUMAZINE, COFACTOR, SUBUNIT.

    Entry informationi

    Entry nameiXDH_BOVIN
    AccessioniPrimary (citable) accession number: P80457
    Secondary accession number(s): Q95325
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 132 of the entry and version 4 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