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P22985

- XDH_RAT

UniProt

P22985 - XDH_RAT

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Protein

Xanthine dehydrogenase/oxidase

Gene

Xdh

Organism
Rattus norvegicus (Rat)
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.1 Publication

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.2 Publications

Sites

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

Regions

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

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB
  2. electron carrier activity Source: InterPro
  3. flavin adenine dinucleotide binding Source: UniProtKB
  4. iron ion binding Source: InterPro
  5. molybdopterin cofactor binding Source: UniProtKB
  6. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro
  7. xanthine dehydrogenase activity Source: UniProtKB
  8. xanthine oxidase activity Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15163.

Names & Taxonomyi

Protein namesi
Recommended name:
Xanthine dehydrogenase/oxidase
Including the following 2 domains:
Xanthine dehydrogenase (EC:1.17.1.4)
Short name:
XD
Xanthine oxidase (EC:1.17.3.2)
Short name:
XO
Alternative name(s):
Xanthine oxidoreductase
Short name:
XOR
Gene namesi
Name:Xdh
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi62043. Xdh.

Subcellular locationi

Peroxisome 1 Publication. Cytoplasm 1 Publication. Secreted By similarity

GO - Cellular componenti

  1. cytosol Source: RGD
  2. extracellular space Source: RGD
  3. peroxisome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome, Secreted

Pathology & Biotechi

Mutagenesis

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

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi535 ↔ 992In oxidase form1 Publication
Glycosylationi1073 – 10731N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Subject to partial proteolysis; this alters the enzyme from the dehydrogenase form (D) to the oxidase form (O).
Contains sulfhydryl groups that are easily oxidized (in vitro); this alters the enzyme from the dehydrogenase form (D) to the oxidase form (O).

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP22985.
PRIDEiP22985.

Expressioni

Inductioni

By interferon.

Gene expression databases

GenevestigatoriP22985.

Interactioni

Subunit structurei

Homodimer. Interacts with BTN1A1 (By similarity).By similarity

Structurei

Secondary structure

1
1331
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 105Combined sources
Beta strandi13 – 175Combined sources
Helixi26 – 327Combined sources
Beta strandi44 – 485Combined sources
Beta strandi52 – 598Combined sources
Turni60 – 634Combined sources
Beta strandi64 – 718Combined sources
Helixi72 – 743Combined sources
Helixi77 – 793Combined sources
Beta strandi84 – 863Combined sources
Helixi88 – 914Combined sources
Beta strandi94 – 963Combined sources
Helixi99 – 1068Combined sources
Helixi116 – 12914Combined sources
Helixi135 – 1406Combined sources
Turni141 – 1444Combined sources
Beta strandi148 – 1503Combined sources
Helixi153 – 1597Combined sources
Helixi160 – 1623Combined sources
Helixi197 – 1993Combined sources
Helixi205 – 2073Combined sources
Helixi213 – 2186Combined sources
Beta strandi226 – 2294Combined sources
Beta strandi234 – 2374Combined sources
Helixi241 – 25010Combined sources
Helixi263 – 2697Combined sources
Beta strandi275 – 2795Combined sources
Helixi284 – 2874Combined sources
Beta strandi289 – 2913Combined sources
Beta strandi293 – 2997Combined sources
Helixi304 – 31714Combined sources
Helixi320 – 3223Combined sources
Helixi324 – 33411Combined sources
Helixi339 – 3424Combined sources
Helixi347 – 3537Combined sources
Helixi361 – 3666Combined sources
Beta strandi370 – 3756Combined sources
Beta strandi378 – 3836Combined sources
Helixi386 – 3883Combined sources
Beta strandi402 – 4098Combined sources
Beta strandi415 – 4228Combined sources
Beta strandi424 – 4285Combined sources
Beta strandi432 – 44110Combined sources
Beta strandi445 – 46117Combined sources
Turni466 – 4683Combined sources
Helixi470 – 4723Combined sources
Beta strandi476 – 4783Combined sources
Helixi479 – 49214Combined sources
Helixi504 – 52825Combined sources
Helixi532 – 5354Combined sources
Helixi540 – 5467Combined sources
Beta strandi555 – 5595Combined sources
Beta strandi565 – 5673Combined 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 strandi645 – 6473Combined 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 – 7104Combined sources
Beta strandi712 – 7176Combined sources
Helixi719 – 7257Combined sources
Beta strandi727 – 73610Combined sources
Beta strandi748 – 7536Combined sources
Beta strandi760 – 7645Combined sources
Helixi769 – 78012Combined sources
Helixi784 – 7863Combined sources
Beta strandi787 – 7926Combined sources
Turni798 – 8014Combined sources
Beta strandi802 – 8043Combined 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
Beta strandi1108 – 11114Combined 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
Turni1250 – 12523Combined sources
Helixi1253 – 12553Combined sources
Helixi1264 – 12674Combined sources
Helixi1268 – 128518Combined sources
Beta strandi1286 – 12894Combined sources
Helixi1301 – 13077Combined sources
Helixi1311 – 13166Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP22985.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 91882Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini228 – 413186FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the xanthine dehydrogenase family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG4630.
HOGENOMiHOG000191197.
HOVERGENiHBG004182.
InParanoidiP22985.
KOiK00106.
PhylomeDBiP22985.

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
IPR022407. OxRdtase_Mopterin_BS.
IPR014307. Xanthine_DH_ssu.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsiTIGR02963. xanthine_xdhA. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22985-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTADELVFFV NGKKVVEKNA DPETTLLVYL RRKLGLCGTK LGCGEGGCGA
60 70 80 90 100
CTVMISKYDR LQNKIVHFSV NACLAPICSL HHVAVTTVEG IGNTQKLHPV
110 120 130 140 150
QERIARSHGS QCGFCTPGIV MSMYTLLRNQ PEPTVEEIEN AFQGNLCRCT
160 170 180 190 200
GYRPILQGFR TFAKDGGCCG GSGNNPNCCM NQTKDQTVSL SPSLFNPEDF
210 220 230 240 250
KPLDPTQEPI FPPELLRLKD TPQKKLRFEG ERVTWIQAST MEELLDLKAQ
260 270 280 290 300
HPDAKLVVGN TEIGIEMKFK NMLFPLIVCP AWIPELNSVV HGPEGISFGA
310 320 330 340 350
SCPLSLVESV LAEEIAKLPE QKTEVFRGVM EQLRWFAGKQ VKSVASIGGN
360 370 380 390 400
IITASPISDL NPVFMASGAK LTLVSRGTRR TVRMDHTFFP GYRKTLLRPE
410 420 430 440 450
EILLSIEIPY SKEGEFFSAF KQASRREDDI AKVTSGMRVL FKPGTIEVQE
460 470 480 490 500
LSLCFGGMAD RTISALKTTP KQLSKSWNEE LLQSVCAGLA EELQLAPDAP
510 520 530 540 550
GGMVEFRRTL TLSFFFKFYL TVLQKLGRAD LEDMCGKLDP TFASATLLFQ
560 570 580 590 600
KDPPANVQLF QEVPKDQSEE DMVGRPLPHL AANMQASGEA VYCDDIPRYE
610 620 630 640 650
NELSLRLVTS TRAHAKITSI DTSEAKKVPG FVCFLTAEDV PNSNATGLFN
660 670 680 690 700
DETVFAKDEV TCVGHIIGAV VADTPEHAQR AARGVKITYE DLPAIITIQD
710 720 730 740 750
AINNNSFYGS EIKIEKGDLK KGFSEADNVV SGELYIGGQE HFYLETNCTI
760 770 780 790 800
AVPKGEAGEM ELFVSTQNTM KTQSFVAKML GVPDNRIVVR VKRMGGGFGG
810 820 830 840 850
KETRSTVVST ALALAAHKTG RPVRCMLDRD EDMLITGGRH PFLAKYKVGF
860 870 880 890 900
MKTGTVVALE VAHFSNGGNT EDLSRSIMER ALFHMDNAYK IPNIRGTGRI
910 920 930 940 950
CKTNLPSNTA FRGFGGPQGM LIAEYWMSEV AITCGLPAEE VRRKNMYKEG
960 970 980 990 1000
DLTHFNQKLE GFTLPRCWDE CIASSQYLAR KREVEKFNRE NCWKKRGLCI
1010 1020 1030 1040 1050
IPTKFGISFT LPFLNQGGAL VHVYTDGSVL LTHGGTEMGQ GLHTKMVQVA
1060 1070 1080 1090 1100
SRALKIPTSK IHISETSTNT VPNTSPTAAS ASADLNGQGV YEACQTILKR
1110 1120 1130 1140 1150
LEPFKKKKPT GPWEAWVMDA YTSAVSLSAT GFYKTPNLGY SFETNSGNPF
1160 1170 1180 1190 1200
HYFSYGVACS EVEIDCLTGD HKNLRTDIVM DVGSSLNPAI DIGQVEGAFV
1210 1220 1230 1240 1250
QGLGLFTMEE LHYSPEGSLH TRGPSTYKIP AFGSIPIEFR VSLLRDCPNK
1260 1270 1280 1290 1300
RAIYASKAVG EPPLFLASSI FFAIKDAIRA ARAQHGDNAK QLFQLDSPAT
1310 1320 1330
PEKIRNACVD QFTTLCVTGV PENCKSWSVR I
Length:1,331
Mass (Da):146,243
Last modified:January 23, 2007 - v3
Checksum:iBF2586A9C63A0B2C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05579 mRNA. Translation: AAA42349.1.
AH000836 Unassigned DNA. Translation: AAA18869.1.
RefSeqiNP_058850.1. NM_017154.1.
UniGeneiRn.202951.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05579 mRNA. Translation: AAA42349.1 .
AH000836 Unassigned DNA. Translation: AAA18869.1 .
RefSeqi NP_058850.1. NM_017154.1.
UniGenei Rn.202951.

3D structure databases

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

Chemistry

BindingDBi P22985.
ChEMBLi CHEMBL1075246.

Proteomic databases

PaxDbi P22985.
PRIDEi P22985.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

CTDi 7498.
RGDi 62043. Xdh.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-15163.

Miscellaneous databases

EvolutionaryTracei P22985.
NextBioi 697781.
PROi P22985.

Gene expression databases

Genevestigatori P22985.

Family and domain databases

Gene3Di 1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProi IPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
IPR022407. OxRdtase_Mopterin_BS.
IPR014307. Xanthine_DH_ssu.
[Graphical view ]
Pfami PF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF000127. Xanthine_DH. 1 hit.
SMARTi SM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view ]
SUPFAMi SSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsi TIGR02963. xanthine_xdhA. 1 hit.
PROSITEi PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

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

Entry informationi

Entry nameiXDH_RAT
AccessioniPrimary (citable) accession number: P22985
Secondary accession number(s): Q63157
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

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

External Data

Dasty 3