Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P80457

- XDH_BOVIN

UniProt

P80457 - XDH_BOVIN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Xanthine dehydrogenase/oxidase

Gene

XDH

Organism
Bos taurus (Bovine)
Status
Reviewed - 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

  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
Complete GO annotation...

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-KW
  2. peroxisome Source: UniProtKB-KW
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.ENSBTAP00000032520.

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 .
PIRi S65135.
RefSeqi NP_776397.1. NM_173972.2.
UniGenei Bt.5403.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 134 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