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Protein

Xanthine dehydrogenase 1

Gene

XDH1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterBy similarityNote: Binds 2 [2Fe-2S] clusters.By similarity
  • FADBy similarity
  • Mo-molybdopterinBy similarityNote: Binds 1 Mo-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: GO_Central
  4. iron ion binding Source: InterPro
  5. molybdopterin cofactor binding Source: GO_Central
  6. oxidoreductase activity, acting on the aldehyde or oxo group of donors Source: GO_Central
  7. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro
  8. xanthine dehydrogenase activity Source: TAIR
  9. xanthine oxidase activity Source: GO_Central

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 catabolic process Source: GO_Central
  6. xanthine metabolic process Source: TAIR
Complete GO annotation...

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. 399.
ReactomeiREACT_301742. Vitamins B6 activation to pyridoxal phosphate.
REACT_323504. 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 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G34890.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: TAIR
Complete GO annotation...

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

« Hide

        10         20         30         40         50
MGSLKKDGEI GDEFTEALLY VNGVRRVLPD GLAHMTLLEY LRDLGLTGTK
60 70 80 90 100
LGCGEGGCGA CTVMVSSYDR KSKTSVHYAV NACLAPLYSV EGMHVISIEG
110 120 130 140 150
LGHRKLGLHP VQESLASSHG SQCGFCTPGF IMSMYSLLRS SKNSPSEEEI
160 170 180 190 200
EECLAGNLCR CTGYRPIVDA FRVFAKSDDA LYCGVSSLSL QDGSTICPST
210 220 230 240 250
GKPCSCGSKT TNEVASCNED RFQSISYSDI DGAKYTDKEL IFPPELLLRK
260 270 280 290 300
LTPLKLRGNG GITWYRPVCL QNLLELKANY PDAKLLVGNT EVGIEMRLKR
310 320 330 340 350
LQYQVLISVA QVPELNALNV NDNGIEVGSA LRLSELLRLF RKIVKERPAH
360 370 380 390 400
ETSACKAFIE QLKWFAGTQI RNVACIGGNI CTASPISDLN PLWMASRAEF
410 420 430 440 450
RITNCNGDVR SIPAKDFFLG YRKVDMGSNE ILLSVFLPWT RPLEYVKEFK
460 470 480 490 500
QAHRRDDDIA IVNGGMRVFL EDKGQQLFVS DASIAYGGVA PLSLCARKTE
510 520 530 540 550
EFLIGKNWNK DLLQDALKVI QSDVVIKEDA PGGMVEFRKS LTLSFFFKFF
560 570 580 590 600
LWVSHNVNNA NSAIETFPPS HMSAVQPVPR LSRIGKQDYE TVKQGTSVGS
610 620 630 640 650
SEVHLSARMQ VTGEAEYTDD TPVPPNTLHA AFVLSKVPHA RILSIDDSAA
660 670 680 690 700
KSSSGFVGLF LAKDIPGDNM IGPIVPDEEL FATDVVTCVG QVIGVVVADT
710 720 730 740 750
HENAKTAAGK VDVRYEELPA ILSIKEAINA KSFHPNTEKR LRKGDVELCF
760 770 780 790 800
QSGQCDRVIE GEVQMGGQEH FYLEPNGSLV WTVDGGSEVH MISSTQAPQK
810 820 830 840 850
HQKYVSHVLG LPMSKVVCKT KRIGGGFGGK ETRSAFIAAA ASVPSYLLNR
860 870 880 890 900
PVKLILDRDV DMMITGHRHS FLGKYKVGFT NEGKILALDL EIYNNGGNSL
910 920 930 940 950
DLSLSVLERA MFHSDNVYEI PHVRIVGNVC FTNFPSNTAF RGFGGPQGML
960 970 980 990 1000
ITENWIQRIA AELNKSPEEI KEMNFQVEGS VTHYCQTLQH CTLHQLWKEL
1010 1020 1030 1040 1050
KVSCNFLKAR READEFNSHN RWKKRGVAMV PTKFGISFTT KFMNQAGALV
1060 1070 1080 1090 1100
HVYTDGTVLV THGGVEMGQG LHTKVAQVAA SAFNIPLSSV FVSETSTDKV
1110 1120 1130 1140 1150
PNASPTAASA SSDMYGAAVL DACEQIIARM EPVASKHNFN TFTELVSACY
1160 1170 1180 1190 1200
FQRIDLSAHG FHIVPDLGFD WISGKGNAFR YYTYGAAFAE VEIDTLTGDF
1210 1220 1230 1240 1250
HTRAADIMLD LGYSLNPAID VGQIEGAFVQ GLGWVALEEL KWGDAAHKWI
1260 1270 1280 1290 1300
KPGSLLTCGP GNYKIPSIND MPFNLNVSLL KGNPNTKAIH SSKAVGEPPF
1310 1320 1330 1340 1350
FLASSVFFAI KEAIKAARTE VGLTDWFPLE SPATPERIRM ACFDEFSAPF
1360
VNSDFYPNLS V
Length:1,361
Mass (Da):149,196
Last modified:February 28, 2003 - v1
Checksum:iBF72FE23A1D59C88
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

STRINGi3702.AT4G34890.1-P.

Proteomic databases

PaxDbiQ8GUQ8.
PRIDEiQ8GUQ8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT4G34890.

Phylogenomic databases

eggNOGiCOG4630.
HOGENOMiHOG000191197.
InParanoidiQ8GUQ8.
KOiK00106.
OMAiCRQIMER.
PhylomeDBiQ8GUQ8.

Enzyme and pathway databases

BioCyciARA:AT4G34890-MONOMER.
MetaCyc:AT4G34890-MONOMER.
BRENDAi1.17.1.4. 399.
ReactomeiREACT_301742. Vitamins B6 activation to pyridoxal phosphate.
REACT_323504. Purine catabolism.

Miscellaneous databases

PROiQ8GUQ8.

Gene expression databases

GenevestigatoriQ8GUQ8.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2003) [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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-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(2004) [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(2006) [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(2007) [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(2009) [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(2009) [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 15, 2012
Last sequence update: February 28, 2003
Last modified: March 31, 2015
This is version 93 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

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 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.