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Protein

Xanthine dehydrogenase/oxidase

Gene

XDH

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

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

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi1.17.1.4. 908.
    1.17.3.2. 908.
    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 Componenti: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    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.ENSBTAP00000016620.

    Structurei

    Secondary structure

    1
    1332
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 105Combined sources
    Beta strandi13 – 175Combined sources
    Helixi26 – 327Combined sources
    Beta strandi44 – 485Combined sources
    Beta strandi52 – 598Combined sources
    Turni60 – 634Combined sources
    Beta strandi64 – 718Combined sources
    Turni72 – 743Combined sources
    Helixi77 – 793Combined sources
    Beta strandi84 – 863Combined sources
    Helixi88 – 903Combined sources
    Beta strandi94 – 963Combined sources
    Helixi100 – 1078Combined sources
    Helixi117 – 13014Combined sources
    Helixi136 – 1405Combined sources
    Turni142 – 1454Combined sources
    Beta strandi149 – 1513Combined sources
    Helixi154 – 1618Combined sources
    Helixi198 – 2003Combined sources
    Helixi206 – 2083Combined sources
    Helixi214 – 2185Combined sources
    Helixi219 – 2213Combined sources
    Beta strandi227 – 2304Combined sources
    Beta strandi235 – 2384Combined sources
    Helixi242 – 25110Combined sources
    Helixi264 – 2707Combined sources
    Beta strandi276 – 2805Combined sources
    Helixi285 – 2873Combined sources
    Beta strandi290 – 2923Combined sources
    Beta strandi294 – 3007Combined sources
    Helixi305 – 31814Combined sources
    Helixi321 – 3233Combined sources
    Helixi325 – 33410Combined sources
    Beta strandi336 – 3383Combined sources
    Helixi340 – 3434Combined sources
    Helixi348 – 3547Combined sources
    Helixi362 – 3676Combined sources
    Beta strandi371 – 3766Combined sources
    Beta strandi379 – 3846Combined sources
    Helixi387 – 3893Combined sources
    Beta strandi403 – 4108Combined sources
    Beta strandi416 – 4227Combined sources
    Beta strandi428 – 4314Combined sources
    Beta strandi435 – 4439Combined sources
    Beta strandi446 – 46217Combined sources
    Helixi467 – 4715Combined sources
    Turni472 – 4754Combined sources
    Beta strandi477 – 4793Combined sources
    Helixi480 – 49314Combined sources
    Helixi505 – 52723Combined sources
    Turni540 – 5423Combined sources
    Helixi543 – 5464Combined sources
    Beta strandi555 – 5595Combined sources
    Helixi582 – 5865Combined sources
    Helixi593 – 5953Combined sources
    Beta strandi603 – 6097Combined sources
    Beta strandi611 – 62111Combined sources
    Helixi625 – 6273Combined sources
    Beta strandi631 – 6355Combined sources
    Helixi637 – 6393Combined sources
    Beta strandi644 – 6474Combined sources
    Beta strandi652 – 6554Combined sources
    Beta strandi658 – 6603Combined sources
    Beta strandi666 – 6749Combined sources
    Helixi675 – 6839Combined sources
    Beta strandi686 – 6916Combined sources
    Helixi698 – 7036Combined sources
    Beta strandi707 – 71711Combined sources
    Helixi719 – 7257Combined sources
    Beta strandi727 – 73610Combined sources
    Beta strandi748 – 7536Combined sources
    Beta strandi760 – 7645Combined sources
    Helixi769 – 78012Combined sources
    Helixi784 – 7863Combined sources
    Beta strandi787 – 7915Combined sources
    Turni798 – 8014Combined sources
    Helixi806 – 81914Combined sources
    Beta strandi823 – 8264Combined sources
    Helixi829 – 8357Combined sources
    Beta strandi842 – 8509Combined sources
    Beta strandi856 – 86611Combined sources
    Helixi874 – 88310Combined sources
    Turni884 – 8885Combined sources
    Beta strandi892 – 90110Combined sources
    Turni912 – 9154Combined sources
    Helixi916 – 93419Combined sources
    Helixi938 – 9458Combined sources
    Helixi964 – 97411Combined sources
    Helixi977 – 99014Combined sources
    Beta strandi992 – 100817Combined sources
    Helixi1012 – 10143Combined sources
    Beta strandi1016 – 10238Combined sources
    Beta strandi1029 – 10346Combined sources
    Beta strandi1038 – 10403Combined sources
    Helixi1042 – 105413Combined sources
    Helixi1058 – 10603Combined sources
    Beta strandi1061 – 10633Combined sources
    Turni1068 – 10703Combined sources
    Turni1079 – 10813Combined sources
    Helixi1082 – 110726Combined sources
    Helixi1113 – 112210Combined sources
    Beta strandi1128 – 11347Combined sources
    Turni1142 – 11454Combined sources
    Beta strandi1151 – 116515Combined sources
    Turni1166 – 11683Combined sources
    Beta strandi1171 – 118111Combined sources
    Helixi1188 – 120720Combined sources
    Turni1224 – 12263Combined sources
    Helixi1232 – 12343Combined sources
    Beta strandi1237 – 12437Combined sources
    Helixi1253 – 12553Combined sources
    Helixi1264 – 12674Combined sources
    Helixi1268 – 128518Combined sources
    Helixi1302 – 13087Combined sources
    Turni1312 – 13143Combined sources
    Helixi1317 – 13193Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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

            10         20         30         40         50
    MTADELVFFV NGKKVVEKNA DPETTLLAYL RRKLGLRGTK LGCGEGGCGA
    60 70 80 90 100
    CTVMLSKYDR LQDKIIHFSA NACLAPICTL HHVAVTTVEG IGSTKTRLHP
    110 120 130 140 150
    VQERIAKSHG SQCGFCTPGI VMSMYTLLRN QPEPTVEEIE DAFQGNLCRC
    160 170 180 190 200
    TGYRPILQGF RTFAKNGGCC GGNGNNPNCC MNQKKDHTVT LSPSLFNPEE
    210 220 230 240 250
    FMPLDPTQEP IFPPELLRLK DVPPKQLRFE GERVTWIQAS TLKELLDLKA
    260 270 280 290 300
    QHPEAKLVVG NTEIGIEMKF KNQLFPMIIC PAWIPELNAV EHGPEGISFG
    310 320 330 340 350
    AACALSSVEK TLLEAVAKLP TQKTEVFRGV LEQLRWFAGK QVKSVASLGG
    360 370 380 390 400
    NIITASPISD LNPVFMASGT KLTIVSRGTR RTVPMDHTFF PSYRKTLLGP
    410 420 430 440 450
    EEILLSIEIP YSREDEFFSA FKQASRREDD IAKVTCGMRV LFQPGSMQVK
    460 470 480 490 500
    ELALCYGGMA DRTISALKTT QKQLSKFWNE KLLQDVCAGL AEELSLSPDA
    510 520 530 540 550
    PGGMIEFRRT LTLSFFFKFY LTVLKKLGKD SKDKCGKLDP TYTSATLLFQ
    560 570 580 590 600
    KDPPANIQLF QEVPNGQSKE DTVGRPLPHL AAAMQASGEA VYCDDIPRYE
    610 620 630 640 650
    NELFLRLVTS TRAHAKIKSI DVSEAQKVPG FVCFLSADDI PGSNETGLFN
    660 670 680 690 700
    DETVFAKDTV TCVGHIIGAV VADTPEHAER AAHVVKVTYE DLPAIITIED
    710 720 730 740 750
    AIKNNSFYGS ELKIEKGDLK KGFSEADNVV SGELYIGGQD HFYLETHCTI
    760 770 780 790 800
    AIPKGEEGEM ELFVSTQNAM KTQSFVAKML GVPVNRILVR VKRMGGGFGG
    810 820 830 840 850
    KETRSTLVSV AVALAAYKTG HPVRCMLDRN EDMLITGGRH PFLARYKVGF
    860 870 880 890 900
    MKTGTIVALE VDHYSNAGNS RDLSHSIMER ALFHMDNCYK IPNIRGTGRL
    910 920 930 940 950
    CKTNLSSNTA FRGFGGPQAL FIAENWMSEV AVTCGLPAEE VRWKNMYKEG
    960 970 980 990 1000
    DLTHFNQRLE GFSVPRCWDE CLKSSQYYAR KSEVDKFNKE NCWKKRGLCI
    1010 1020 1030 1040 1050
    IPTKFGISFT VPFLNQAGAL IHVYTDGSVL VSHGGTEMGQ GLHTKMVQVA
    1060 1070 1080 1090 1100
    SKALKIPISK IYISETSTNT VPNSSPTAAS VSTDIYGQAV YEACQTILKR
    1110 1120 1130 1140 1150
    LEPFKKKNPD GSWEDWVMAA YQDRVSLSTT GFYRTPNLGY SFETNSGNAF
    1160 1170 1180 1190 1200
    HYFTYGVACS EVEIDCLTGD HKNLRTDIVM DVGSSLNPAI DIGQVEGAFV
    1210 1220 1230 1240 1250
    QGLGLFTLEE LHYSPEGSLH TRGPSTYKIP AFGSIPTEFR VSLLRDCPNK
    1260 1270 1280 1290 1300
    KAIYASKAVG EPPLFLGASV FFAIKDAIRA ARAQHTNNNT KELFRLDSPA
    1310 1320 1330
    TPEKIRNACV DKFTTLCVTG APGNCKPWSL RV
    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:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X83508 mRNA. Translation: CAA58497.1.
    X98491 mRNA. Translation: CAA67117.1.
    PIRiS65135.
    RefSeqiNP_776397.1. NM_173972.2.
    UniGeneiBt.5403.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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...

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000016620.

    Chemistry

    BindingDBiP80457.
    ChEMBLiCHEMBL3649.

    Proteomic databases

    PaxDbiP80457.
    PRIDEiP80457.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi280960.
    KEGGibta:280960.

    Organism-specific databases

    CTDi7498.

    Phylogenomic databases

    eggNOGiCOG4630.
    HOGENOMiHOG000191197.
    HOVERGENiHBG004182.
    InParanoidiP80457.
    KOiK00106.

    Enzyme and pathway databases

    BRENDAi1.17.1.4. 908.
    1.17.3.2. 908.
    SABIO-RKP80457.

    Miscellaneous databases

    EvolutionaryTraceiP80457.
    NextBioi20805070.
    PROiP80457.

    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]
    ProtoNetiSearch...

    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: June 24, 2015
    This is version 138 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.