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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.By similarity

Catalytic activityi

Xanthine + NAD+ + H2O = urate + NADH.4 Publications
Hypoxanthine + NAD+ + H2O = xanthine + NADH.4 Publications
Xanthine + H2O + O2 = urate + H2O2.4 Publications

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)DescriptionActionsGraphical viewLength
    Metal bindingi43Iron-sulfur 11
    Metal bindingi48Iron-sulfur 11
    Metal bindingi51Iron-sulfur 11
    Metal bindingi73Iron-sulfur 11
    Metal bindingi113Iron-sulfur 21
    Metal bindingi116Iron-sulfur 21
    Metal bindingi148Iron-sulfur 21
    Metal bindingi150Iron-sulfur 21
    Binding sitei337FAD2 Publications1
    Binding sitei360FAD2 Publications1
    Binding sitei404FAD; via amide nitrogen and carbonyl oxygen2 Publications1
    Binding sitei422FAD2 Publications1
    Metal bindingi767Molybdenum1
    Metal bindingi798Molybdenum; via carbonyl oxygen1
    Binding sitei802Substrate1
    Binding sitei880Substrate1
    Metal bindingi912Molybdenum; via amide nitrogen1
    Binding sitei914Substrate1
    Binding sitei1010Substrate; via amide nitrogen1
    Metal bindingi1079Molybdenum; via amide nitrogen1
    Active sitei1261Proton acceptor1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi257 – 264FAD2 Publications8
    Nucleotide bindingi347 – 351FAD2 Publications5

    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:1.17.1.44 Publications)
    Short name:
    XD
    Xanthine oxidase (EC:1.17.3.24 Publications)
    Short name:
    XO
    Alternative name(s):
    Xanthine oxidoreductase
    Short name:
    XOR
    Gene namesi
    Name:XDH
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    Proteomesi
    • UP000009136 Componenti: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Peroxisome, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi335R → 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 Publication1
    Mutagenesisi336W → 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 Publication1
    Mutagenesisi427R → 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 Publication1

    Chemistry databases

    ChEMBLiCHEMBL3649.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001660822 – 1332Xanthine dehydrogenase/oxidaseAdd BLAST1331

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi535 ↔ 992In oxidase formBy similarity
    Glycosylationi1073N-linked (GlcNAc...)Sequence analysis1

    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.
    PeptideAtlasiP80457.
    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.

    Chemistry databases

    BindingDBiP80457.

    Structurei

    Secondary structure

    11332
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi6 – 10Combined sources5
    Beta strandi13 – 17Combined sources5
    Helixi26 – 32Combined sources7
    Beta strandi44 – 48Combined sources5
    Beta strandi52 – 59Combined sources8
    Turni60 – 63Combined sources4
    Beta strandi64 – 71Combined sources8
    Turni72 – 74Combined sources3
    Helixi77 – 79Combined sources3
    Beta strandi84 – 86Combined sources3
    Helixi88 – 90Combined sources3
    Beta strandi94 – 96Combined sources3
    Helixi100 – 107Combined sources8
    Helixi117 – 130Combined sources14
    Helixi136 – 140Combined sources5
    Turni142 – 145Combined sources4
    Beta strandi149 – 151Combined sources3
    Helixi154 – 161Combined sources8
    Helixi198 – 200Combined sources3
    Helixi206 – 208Combined sources3
    Helixi214 – 218Combined sources5
    Helixi219 – 221Combined sources3
    Beta strandi227 – 230Combined sources4
    Beta strandi235 – 238Combined sources4
    Helixi242 – 251Combined sources10
    Helixi264 – 270Combined sources7
    Beta strandi276 – 280Combined sources5
    Helixi285 – 287Combined sources3
    Beta strandi290 – 292Combined sources3
    Beta strandi294 – 300Combined sources7
    Helixi305 – 318Combined sources14
    Helixi321 – 323Combined sources3
    Helixi325 – 334Combined sources10
    Beta strandi336 – 338Combined sources3
    Helixi340 – 343Combined sources4
    Helixi348 – 354Combined sources7
    Helixi362 – 367Combined sources6
    Beta strandi371 – 376Combined sources6
    Beta strandi379 – 384Combined sources6
    Helixi387 – 389Combined sources3
    Beta strandi403 – 410Combined sources8
    Beta strandi416 – 422Combined sources7
    Beta strandi428 – 431Combined sources4
    Beta strandi435 – 443Combined sources9
    Beta strandi446 – 462Combined sources17
    Helixi467 – 471Combined sources5
    Turni472 – 475Combined sources4
    Beta strandi477 – 479Combined sources3
    Helixi480 – 493Combined sources14
    Helixi505 – 527Combined sources23
    Turni540 – 542Combined sources3
    Helixi543 – 546Combined sources4
    Beta strandi555 – 559Combined sources5
    Helixi582 – 586Combined sources5
    Helixi593 – 595Combined sources3
    Beta strandi603 – 609Combined sources7
    Beta strandi611 – 621Combined sources11
    Helixi625 – 627Combined sources3
    Beta strandi631 – 635Combined sources5
    Helixi637 – 639Combined sources3
    Beta strandi644 – 647Combined sources4
    Beta strandi652 – 655Combined sources4
    Beta strandi658 – 660Combined sources3
    Beta strandi666 – 674Combined sources9
    Helixi675 – 683Combined sources9
    Beta strandi686 – 691Combined sources6
    Helixi698 – 703Combined sources6
    Beta strandi707 – 717Combined sources11
    Helixi719 – 725Combined sources7
    Beta strandi727 – 736Combined sources10
    Beta strandi748 – 753Combined sources6
    Beta strandi760 – 764Combined sources5
    Helixi769 – 780Combined sources12
    Helixi784 – 786Combined sources3
    Beta strandi787 – 791Combined sources5
    Turni798 – 801Combined sources4
    Helixi806 – 819Combined sources14
    Beta strandi823 – 826Combined sources4
    Helixi829 – 835Combined sources7
    Beta strandi842 – 850Combined sources9
    Beta strandi856 – 866Combined sources11
    Helixi874 – 883Combined sources10
    Turni884 – 888Combined sources5
    Beta strandi892 – 901Combined sources10
    Turni912 – 915Combined sources4
    Helixi916 – 934Combined sources19
    Helixi938 – 945Combined sources8
    Helixi964 – 974Combined sources11
    Helixi977 – 990Combined sources14
    Beta strandi992 – 1008Combined sources17
    Helixi1012 – 1014Combined sources3
    Beta strandi1016 – 1023Combined sources8
    Beta strandi1029 – 1034Combined sources6
    Beta strandi1038 – 1040Combined sources3
    Helixi1042 – 1054Combined sources13
    Helixi1058 – 1060Combined sources3
    Beta strandi1061 – 1063Combined sources3
    Turni1068 – 1070Combined sources3
    Turni1079 – 1081Combined sources3
    Helixi1082 – 1107Combined sources26
    Helixi1113 – 1122Combined sources10
    Beta strandi1128 – 1134Combined sources7
    Turni1142 – 1145Combined sources4
    Beta strandi1151 – 1165Combined sources15
    Turni1166 – 1168Combined sources3
    Beta strandi1171 – 1181Combined sources11
    Helixi1188 – 1207Combined sources20
    Turni1224 – 1226Combined sources3
    Helixi1232 – 1234Combined sources3
    Beta strandi1237 – 1243Combined sources7
    Helixi1253 – 1255Combined sources3
    Helixi1264 – 1267Combined sources4
    Helixi1268 – 1285Combined sources18
    Helixi1302 – 1308Combined sources7
    Turni1312 – 1314Combined sources3
    Helixi1317 – 1319Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP80457.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini4 – 912Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST88
    Domaini229 – 414FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST186

    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

    eggNOGiKOG0430. Eukaryota.
    COG4630. LUCA.
    COG4631. LUCA.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti188T → TQ in CAA67117 (PubMed:9388547).Curated1
    Sequence conflicti199E → K in CAA67117 (PubMed:9388547).Curated1
    Sequence conflicti366M → V in CAA67117 (PubMed:9388547).Curated1
    Sequence conflicti552D → H in CAA58497 (PubMed:8708081).Curated1
    Sequence conflicti958R → K in CAA67117 (PubMed:9388547).Curated1
    Sequence conflicti976Q → E in CAA67117 (PubMed:9388547).Curated1
    Sequence conflicti1039 – 1040GQ → E in CAA67117 (PubMed:9388547).Curated2
    Sequence conflicti1244L → V in CAA67117 (PubMed:9388547).Curated1
    Sequence conflicti1268A → P in CAA67117 (PubMed:9388547).Curated1
    Sequence conflicti1279 – 1281RAA → ARG in CAA67117 (PubMed:9388547).Curated3

    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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000016620.

    Chemistry databases

    BindingDBiP80457.
    ChEMBLiCHEMBL3649.

    Proteomic databases

    PaxDbiP80457.
    PeptideAtlasiP80457.
    PRIDEiP80457.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi280960.
    KEGGibta:280960.

    Organism-specific databases

    CTDi7498.

    Phylogenomic databases

    eggNOGiKOG0430. Eukaryota.
    COG4630. LUCA.
    COG4631. LUCA.
    HOGENOMiHOG000191197.
    HOVERGENiHBG004182.
    InParanoidiP80457.
    KOiK00106.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTraceiP80457.
    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...

    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: November 2, 2016
    This is version 149 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

    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 one 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.