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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

Binds 2 2Fe-2S clusters.
FAD.
Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

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 – 105
Beta strandi13 – 175
Helixi26 – 327
Beta strandi44 – 485
Beta strandi52 – 598
Turni60 – 634
Beta strandi64 – 718
Helixi72 – 743
Helixi77 – 793
Beta strandi84 – 863
Helixi88 – 914
Beta strandi94 – 963
Helixi99 – 1068
Helixi116 – 12914
Helixi135 – 1406
Turni141 – 1444
Beta strandi148 – 1503
Helixi153 – 1597
Helixi160 – 1623
Helixi197 – 1993
Helixi205 – 2073
Helixi213 – 2186
Beta strandi226 – 2294
Beta strandi234 – 2374
Helixi241 – 25010
Helixi263 – 2697
Beta strandi275 – 2795
Helixi284 – 2874
Beta strandi289 – 2913
Beta strandi293 – 2997
Helixi304 – 31714
Helixi320 – 3223
Helixi324 – 33411
Helixi339 – 3424
Helixi347 – 3537
Helixi361 – 3666
Beta strandi370 – 3756
Beta strandi378 – 3836
Helixi386 – 3883
Beta strandi402 – 4098
Beta strandi415 – 4228
Beta strandi424 – 4285
Beta strandi432 – 44110
Beta strandi445 – 46117
Turni466 – 4683
Helixi470 – 4723
Beta strandi476 – 4783
Helixi479 – 49214
Helixi504 – 52825
Helixi532 – 5354
Helixi540 – 5467
Beta strandi555 – 5595
Beta strandi565 – 5673
Helixi582 – 5865
Helixi593 – 5953
Beta strandi603 – 6097
Beta strandi611 – 62111
Helixi625 – 6273
Beta strandi631 – 6355
Helixi637 – 6393
Beta strandi645 – 6473
Beta strandi652 – 6554
Beta strandi658 – 6603
Beta strandi666 – 6749
Helixi675 – 6839
Beta strandi686 – 6916
Helixi698 – 7036
Beta strandi707 – 7104
Beta strandi712 – 7176
Helixi719 – 7257
Beta strandi727 – 73610
Beta strandi748 – 7536
Beta strandi760 – 7645
Helixi769 – 78012
Helixi784 – 7863
Beta strandi787 – 7926
Turni798 – 8014
Beta strandi802 – 8043
Helixi806 – 81914
Beta strandi823 – 8264
Helixi829 – 8357
Beta strandi842 – 8509
Beta strandi856 – 86611
Helixi874 – 88310
Turni884 – 8885
Beta strandi892 – 90110
Turni912 – 9154
Helixi916 – 93419
Helixi938 – 9458
Helixi964 – 97411
Helixi977 – 99014
Beta strandi992 – 100817
Helixi1012 – 10143
Beta strandi1016 – 10238
Beta strandi1029 – 10346
Beta strandi1038 – 10403
Helixi1042 – 105413
Helixi1058 – 10603
Beta strandi1061 – 10633
Turni1068 – 10703
Turni1079 – 10813
Helixi1082 – 110726
Beta strandi1108 – 11114
Helixi1113 – 112210
Beta strandi1128 – 11347
Turni1142 – 11454
Beta strandi1151 – 116515
Turni1166 – 11683
Beta strandi1171 – 118111
Helixi1188 – 120720
Turni1224 – 12263
Helixi1232 – 12343
Beta strandi1237 – 12437
Turni1250 – 12523
Helixi1253 – 12553
Helixi1264 – 12674
Helixi1268 – 128518
Beta strandi1286 – 12894
Helixi1301 – 13077
Helixi1311 – 13166

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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: October 29, 2014
This is version 137 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