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Q8GUQ8

- XDH1_ARATH

UniProt

Q8GUQ8 - XDH1_ARATH

Protein

Xanthine dehydrogenase 1

Gene

XDH1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Key enzyme involved in purine catabolism. Catalyzes the oxidation of hypoxanthine to xanthine and the oxidation of xanthine to urate. Regulates the level of ureides and plays an important role during plant growth and development, senescence and response to stresses. Possesses NADH oxidase activity and may contribute to the generation of superoxide anions in planta.6 Publications

    Catalytic activityi

    Xanthine + NAD+ + H2O = urate + NADH.1 Publication
    Hypoxanthine + NAD+ + H2O = xanthine + NADH.1 Publication

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi53 – 531Iron-sulfur (2Fe-2S) 1PROSITE-ProRule annotation
    Metal bindingi58 – 581Iron-sulfur (2Fe-2S) 1PROSITE-ProRule annotation
    Metal bindingi61 – 611Iron-sulfur (2Fe-2S) 1PROSITE-ProRule annotation
    Metal bindingi83 – 831Iron-sulfur (2Fe-2S) 1PROSITE-ProRule annotation
    Metal bindingi123 – 1231Iron-sulfur (2Fe-2S) 2PROSITE-ProRule annotation
    Metal bindingi126 – 1261Iron-sulfur (2Fe-2S) 2PROSITE-ProRule annotation
    Metal bindingi159 – 1591Iron-sulfur (2Fe-2S) 2PROSITE-ProRule annotation
    Metal bindingi161 – 1611Iron-sulfur (2Fe-2S) 2PROSITE-ProRule annotation
    Binding sitei365 – 3651FADBy similarity
    Binding sitei388 – 3881FADBy similarity
    Binding sitei432 – 4321FAD; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei450 – 4501FADBy similarity
    Metal bindingi796 – 7961MolybdenumBy similarity
    Metal bindingi827 – 8271Molybdenum; via carbonyl oxygenBy similarity
    Binding sitei831 – 8311SubstrateBy similarity
    Binding sitei909 – 9091SubstrateBy similarity
    Metal bindingi941 – 9411Molybdenum; via amide nitrogenBy similarity
    Binding sitei943 – 9431SubstrateBy similarity
    Binding sitei1039 – 10391SubstrateBy similarity
    Metal bindingi1108 – 11081Molybdenum; via amide nitrogenBy similarity
    Active sitei1297 – 12971Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi285 – 2928FADBy similarity
    Nucleotide bindingi375 – 3795FADBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. purine nucleobase catabolic process Source: TAIR
    2. response to reactive oxygen species Source: TAIR
    3. response to water deprivation Source: TAIR
    4. superoxide anion generation Source: TAIR
    5. xanthine metabolic process Source: TAIR

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciARA:AT4G34890-MONOMER.
    MetaCyc:AT4G34890-MONOMER.
    BRENDAi1.17.1.4. 302.
    ReactomeiREACT_187833. Vitamins B6 activation to pyridoxal phosphate.
    REACT_219858. Purine catabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Xanthine dehydrogenase 1 (EC:1.17.1.4)
    Short name:
    AtXDH1
    Gene namesi
    Name:XDH1
    Ordered Locus Names:At4g34890
    ORF Names:T11I11.130
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G34890.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: TAIR

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi364 – 3641W → A: Decreases activity 8-fold. 1 Publication
    Mutagenesisi421 – 4211Y → A: Decreases activity 4-fold. 1 Publication
    Mutagenesisi831 – 8311E → A: Loss of activity. 1 Publication
    Mutagenesisi909 – 9091R → A: Decreases activity 12-fold. 1 Publication
    Mutagenesisi1297 – 12971E → A: Decreases activity 40-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13611361Xanthine dehydrogenase 1PRO_0000417457Add
    BLAST

    Proteomic databases

    PaxDbiQ8GUQ8.
    PRIDEiQ8GUQ8.

    Expressioni

    Tissue specificityi

    Expressed in roots, leaves, stems, flowers and siliques.1 Publication

    Inductioni

    By salt and drought stresses, and abscisic (ABA) treatment. Down-regulated by cold and freezing stresses.2 Publications

    Gene expression databases

    GenevestigatoriQ8GUQ8.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi3702.AT4G34890.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8GUQ8.
    SMRiQ8GUQ8. Positions 16-176, 238-553, 597-1347.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini15 – 101872Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini257 – 442186FAD-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.
    InParanoidiQ8GUQ8.
    KOiK00106.
    OMAiCRQIMER.
    PhylomeDBiQ8GUQ8.

    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.
    [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.
    PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
    PS51085. 2FE2S_FER_2. 1 hit.
    PS51387. FAD_PCMH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8GUQ8-1 [UniParc]FASTAAdd to Basket

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    MGSLKKDGEI GDEFTEALLY VNGVRRVLPD GLAHMTLLEY LRDLGLTGTK     50
    LGCGEGGCGA CTVMVSSYDR KSKTSVHYAV NACLAPLYSV EGMHVISIEG 100
    LGHRKLGLHP VQESLASSHG SQCGFCTPGF IMSMYSLLRS SKNSPSEEEI 150
    EECLAGNLCR CTGYRPIVDA FRVFAKSDDA LYCGVSSLSL QDGSTICPST 200
    GKPCSCGSKT TNEVASCNED RFQSISYSDI DGAKYTDKEL IFPPELLLRK 250
    LTPLKLRGNG GITWYRPVCL QNLLELKANY PDAKLLVGNT EVGIEMRLKR 300
    LQYQVLISVA QVPELNALNV NDNGIEVGSA LRLSELLRLF RKIVKERPAH 350
    ETSACKAFIE QLKWFAGTQI RNVACIGGNI CTASPISDLN PLWMASRAEF 400
    RITNCNGDVR SIPAKDFFLG YRKVDMGSNE ILLSVFLPWT RPLEYVKEFK 450
    QAHRRDDDIA IVNGGMRVFL EDKGQQLFVS DASIAYGGVA PLSLCARKTE 500
    EFLIGKNWNK DLLQDALKVI QSDVVIKEDA PGGMVEFRKS LTLSFFFKFF 550
    LWVSHNVNNA NSAIETFPPS HMSAVQPVPR LSRIGKQDYE TVKQGTSVGS 600
    SEVHLSARMQ VTGEAEYTDD TPVPPNTLHA AFVLSKVPHA RILSIDDSAA 650
    KSSSGFVGLF LAKDIPGDNM IGPIVPDEEL FATDVVTCVG QVIGVVVADT 700
    HENAKTAAGK VDVRYEELPA ILSIKEAINA KSFHPNTEKR LRKGDVELCF 750
    QSGQCDRVIE GEVQMGGQEH FYLEPNGSLV WTVDGGSEVH MISSTQAPQK 800
    HQKYVSHVLG LPMSKVVCKT KRIGGGFGGK ETRSAFIAAA ASVPSYLLNR 850
    PVKLILDRDV DMMITGHRHS FLGKYKVGFT NEGKILALDL EIYNNGGNSL 900
    DLSLSVLERA MFHSDNVYEI PHVRIVGNVC FTNFPSNTAF RGFGGPQGML 950
    ITENWIQRIA AELNKSPEEI KEMNFQVEGS VTHYCQTLQH CTLHQLWKEL 1000
    KVSCNFLKAR READEFNSHN RWKKRGVAMV PTKFGISFTT KFMNQAGALV 1050
    HVYTDGTVLV THGGVEMGQG LHTKVAQVAA SAFNIPLSSV FVSETSTDKV 1100
    PNASPTAASA SSDMYGAAVL DACEQIIARM EPVASKHNFN TFTELVSACY 1150
    FQRIDLSAHG FHIVPDLGFD WISGKGNAFR YYTYGAAFAE VEIDTLTGDF 1200
    HTRAADIMLD LGYSLNPAID VGQIEGAFVQ GLGWVALEEL KWGDAAHKWI 1250
    KPGSLLTCGP GNYKIPSIND MPFNLNVSLL KGNPNTKAIH SSKAVGEPPF 1300
    FLASSVFFAI KEAIKAARTE VGLTDWFPLE SPATPERIRM ACFDEFSAPF 1350
    VNSDFYPNLS V 1361
    Length:1,361
    Mass (Da):149,196
    Last modified:March 1, 2003 - v1
    Checksum:iBF72FE23A1D59C88
    GO

    Sequence cautioni

    The sequence CAB45450.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAB80206.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY171562 mRNA. Translation: AAO11781.1.
    AL079347 Genomic DNA. Translation: CAB45450.1. Sequence problems.
    AL161586 Genomic DNA. Translation: CAB80206.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE86434.1.
    PIRiT10235.
    RefSeqiNP_195215.2. NM_119655.3.
    UniGeneiAt.27839.

    Genome annotation databases

    EnsemblPlantsiAT4G34890.1; AT4G34890.1; AT4G34890.
    GeneIDi829641.
    KEGGiath:AT4G34890.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY171562 mRNA. Translation: AAO11781.1 .
    AL079347 Genomic DNA. Translation: CAB45450.1 . Sequence problems.
    AL161586 Genomic DNA. Translation: CAB80206.1 . Sequence problems.
    CP002687 Genomic DNA. Translation: AEE86434.1 .
    PIRi T10235.
    RefSeqi NP_195215.2. NM_119655.3.
    UniGenei At.27839.

    3D structure databases

    ProteinModelPortali Q8GUQ8.
    SMRi Q8GUQ8. Positions 16-176, 238-553, 597-1347.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT4G34890.1-P.

    Proteomic databases

    PaxDbi Q8GUQ8.
    PRIDEi Q8GUQ8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G34890.1 ; AT4G34890.1 ; AT4G34890 .
    GeneIDi 829641.
    KEGGi ath:AT4G34890.

    Organism-specific databases

    TAIRi AT4G34890.

    Phylogenomic databases

    eggNOGi COG4630.
    HOGENOMi HOG000191197.
    InParanoidi Q8GUQ8.
    KOi K00106.
    OMAi CRQIMER.
    PhylomeDBi Q8GUQ8.

    Enzyme and pathway databases

    BioCyci ARA:AT4G34890-MONOMER.
    MetaCyc:AT4G34890-MONOMER.
    BRENDAi 1.17.1.4. 302.
    Reactomei REACT_187833. Vitamins B6 activation to pyridoxal phosphate.
    REACT_219858. Purine catabolism.

    Miscellaneous databases

    PROi Q8GUQ8.

    Gene expression databases

    Genevestigatori Q8GUQ8.

    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.
    [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.
    PROSITEi PS00197. 2FE2S_FER_1. 1 hit.
    PS51085. 2FE2S_FER_2. 1 hit.
    PS51387. FAD_PCMH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Tandem orientation of duplicated xanthine dehydrogenase genes from Arabidopsis thaliana: differential gene expression and enzyme activities."
      Hesberg C., Haensch R., Mendel R.R., Bittner F.
      J. Biol. Chem. 279:13547-13554(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, TISSUE SPECIFICITY, INDUCTION.
    2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "The plant Mo-hydroxylases aldehyde oxidase and xanthine dehydrogenase have distinct reactive oxygen species signatures and are induced by drought and abscisic acid."
      Yesbergenova Z., Yang G., Oron E., Soffer D., Fluhr R., Sagi M.
      Plant J. 42:862-876(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    5. "The RNAi-mediated silencing of xanthine dehydrogenase impairs growth and fertility and accelerates leaf senescence in transgenic Arabidopsis plants."
      Nakagawa A., Sakamoto S., Takahashi M., Morikawa H., Sakamoto A.
      Plant Cell Physiol. 48:1484-1495(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "A critical role for ureides in dark and senescence-induced purine remobilization is unmasked in the Atxdh1 Arabidopsis mutant."
      Brychkova G., Alikulov Z., Fluhr R., Sagi M.
      Plant J. 54:496-509(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "RNA interference-mediated suppression of xanthine dehydrogenase reveals the role of purine metabolism in drought tolerance in Arabidopsis."
      Watanabe S., Nakagawa A., Izumi S., Shimada H., Sakamoto A.
      FEBS Lett. 584:1181-1186(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Xanthine dehydrogenase AtXDH1 from Arabidopsis thaliana is a potent producer of superoxide anions via its NADH oxidase activity."
      Zarepour M., Kaspari K., Stagge S., Rethmeier R., Mendel R.R., Bittner F.
      Plant Mol. Biol. 72:301-310(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF TRP-364; TYR-421; GLU-831; ARG-909 AND GLU-1297.

    Entry informationi

    Entry nameiXDH1_ARATH
    AccessioniPrimary (citable) accession number: Q8GUQ8
    Secondary accession number(s): Q9SW46
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2012
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Plants silencing simultaneously XDH1 and XDH2 show reduced growth, impaired silique development, increased seed sterility, precocious senescence of mature leaves and overaccumulation of xanthine.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3