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Q8GUQ8 (XDH1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Xanthine dehydrogenase 1

Short name=AtXDH1
EC=1.17.1.4
Gene names
Name:XDH1
Ordered Locus Names:At4g34890
ORF Names:T11I11.130
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1361 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Catalytic activity

Xanthine + NAD+ + H2O = urate + NADH. Ref.1

Hypoxanthine + NAD+ + H2O = xanthine + NADH. Ref.1

Cofactor

Binds 2 2Fe-2S clusters By similarity.

FAD By similarity.

Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per subunit By similarity.

Subunit structure

Homodimer Probable. Ref.1

Tissue specificity

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

Induction

By salt and drought stresses, and abscisic (ABA) treatment. Down-regulated by cold and freezing stresses. Ref.1 Ref.4

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 (Ref.5).

Sequence similarities

Belongs to the xanthine dehydrogenase family.

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 FAD-binding PCMH-type domain.

Sequence caution

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13611361Xanthine dehydrogenase 1
PRO_0000417457

Regions

Domain15 – 101872Fe-2S ferredoxin-type
Domain257 – 442186FAD-binding PCMH-type
Nucleotide binding285 – 2928FAD By similarity
Nucleotide binding375 – 3795FAD By similarity

Sites

Active site12971Proton acceptor By similarity
Metal binding531Iron-sulfur (2Fe-2S) 1 By similarity
Metal binding581Iron-sulfur (2Fe-2S) 1 By similarity
Metal binding611Iron-sulfur (2Fe-2S) 1 By similarity
Metal binding831Iron-sulfur (2Fe-2S) 1 By similarity
Metal binding1231Iron-sulfur (2Fe-2S) 2 By similarity
Metal binding1261Iron-sulfur (2Fe-2S) 2 By similarity
Metal binding1591Iron-sulfur (2Fe-2S) 2 By similarity
Metal binding1611Iron-sulfur (2Fe-2S) 2 By similarity
Metal binding7961Molybdenum By similarity
Metal binding8271Molybdenum; via carbonyl oxygen By similarity
Metal binding9411Molybdenum; via amide nitrogen By similarity
Metal binding11081Molybdenum; via amide nitrogen By similarity
Binding site3651FAD By similarity
Binding site3881FAD By similarity
Binding site4321FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site4501FAD By similarity
Binding site8311Substrate By similarity
Binding site9091Substrate By similarity
Binding site9431Substrate By similarity
Binding site10391Substrate By similarity

Experimental info

Mutagenesis3641W → A: Decreases activity 8-fold. Ref.8
Mutagenesis4211Y → A: Decreases activity 4-fold. Ref.8
Mutagenesis8311E → A: Loss of activity. Ref.8
Mutagenesis9091R → A: Decreases activity 12-fold. Ref.8
Mutagenesis12971E → A: Decreases activity 40-fold. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Q8GUQ8 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: BF72FE23A1D59C88

FASTA1,361149,196
        10         20         30         40         50         60 
MGSLKKDGEI GDEFTEALLY VNGVRRVLPD GLAHMTLLEY LRDLGLTGTK LGCGEGGCGA 

        70         80         90        100        110        120 
CTVMVSSYDR KSKTSVHYAV NACLAPLYSV EGMHVISIEG LGHRKLGLHP VQESLASSHG 

       130        140        150        160        170        180 
SQCGFCTPGF IMSMYSLLRS SKNSPSEEEI EECLAGNLCR CTGYRPIVDA FRVFAKSDDA 

       190        200        210        220        230        240 
LYCGVSSLSL QDGSTICPST GKPCSCGSKT TNEVASCNED RFQSISYSDI DGAKYTDKEL 

       250        260        270        280        290        300 
IFPPELLLRK LTPLKLRGNG GITWYRPVCL QNLLELKANY PDAKLLVGNT EVGIEMRLKR 

       310        320        330        340        350        360 
LQYQVLISVA QVPELNALNV NDNGIEVGSA LRLSELLRLF RKIVKERPAH ETSACKAFIE 

       370        380        390        400        410        420 
QLKWFAGTQI RNVACIGGNI CTASPISDLN PLWMASRAEF RITNCNGDVR SIPAKDFFLG 

       430        440        450        460        470        480 
YRKVDMGSNE ILLSVFLPWT RPLEYVKEFK QAHRRDDDIA IVNGGMRVFL EDKGQQLFVS 

       490        500        510        520        530        540 
DASIAYGGVA PLSLCARKTE EFLIGKNWNK DLLQDALKVI QSDVVIKEDA PGGMVEFRKS 

       550        560        570        580        590        600 
LTLSFFFKFF LWVSHNVNNA NSAIETFPPS HMSAVQPVPR LSRIGKQDYE TVKQGTSVGS 

       610        620        630        640        650        660 
SEVHLSARMQ VTGEAEYTDD TPVPPNTLHA AFVLSKVPHA RILSIDDSAA KSSSGFVGLF 

       670        680        690        700        710        720 
LAKDIPGDNM IGPIVPDEEL FATDVVTCVG QVIGVVVADT HENAKTAAGK VDVRYEELPA 

       730        740        750        760        770        780 
ILSIKEAINA KSFHPNTEKR LRKGDVELCF QSGQCDRVIE GEVQMGGQEH FYLEPNGSLV 

       790        800        810        820        830        840 
WTVDGGSEVH MISSTQAPQK HQKYVSHVLG LPMSKVVCKT KRIGGGFGGK ETRSAFIAAA 

       850        860        870        880        890        900 
ASVPSYLLNR PVKLILDRDV DMMITGHRHS FLGKYKVGFT NEGKILALDL EIYNNGGNSL 

       910        920        930        940        950        960 
DLSLSVLERA MFHSDNVYEI PHVRIVGNVC FTNFPSNTAF RGFGGPQGML ITENWIQRIA 

       970        980        990       1000       1010       1020 
AELNKSPEEI KEMNFQVEGS VTHYCQTLQH CTLHQLWKEL KVSCNFLKAR READEFNSHN 

      1030       1040       1050       1060       1070       1080 
RWKKRGVAMV PTKFGISFTT KFMNQAGALV HVYTDGTVLV THGGVEMGQG LHTKVAQVAA 

      1090       1100       1110       1120       1130       1140 
SAFNIPLSSV FVSETSTDKV PNASPTAASA SSDMYGAAVL DACEQIIARM EPVASKHNFN 

      1150       1160       1170       1180       1190       1200 
TFTELVSACY FQRIDLSAHG FHIVPDLGFD WISGKGNAFR YYTYGAAFAE VEIDTLTGDF 

      1210       1220       1230       1240       1250       1260 
HTRAADIMLD LGYSLNPAID VGQIEGAFVQ GLGWVALEEL KWGDAAHKWI KPGSLLTCGP 

      1270       1280       1290       1300       1310       1320 
GNYKIPSIND MPFNLNVSLL KGNPNTKAIH SSKAVGEPPF FLASSVFFAI KEAIKAARTE 

      1330       1340       1350       1360 
VGLTDWFPLE SPATPERIRM ACFDEFSAPF VNSDFYPNLS V 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT10235.
RefSeqNP_195215.2. NM_119655.3.
UniGeneAt.27839.

3D structure databases

ProteinModelPortalQ8GUQ8.
SMRQ8GUQ8. Positions 16-176, 238-553, 597-1347.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G34890.1-P.

Proteomic databases

PaxDbQ8GUQ8.
PRIDEQ8GUQ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G34890.1; AT4G34890.1; AT4G34890.
GeneID829641.
KEGGath:AT4G34890.

Organism-specific databases

TAIRAT4G34890.

Phylogenomic databases

eggNOGCOG4630.
HOGENOMHOG000191197.
InParanoidQ8GUQ8.
KOK00106.
OMACRQIMER.
PhylomeDBQ8GUQ8.

Enzyme and pathway databases

BioCycARA:AT4G34890-MONOMER.
MetaCyc:AT4G34890-MONOMER.
BRENDA1.17.1.4. 302.

Gene expression databases

GenevestigatorQ8GUQ8.

Family and domain databases

Gene3D1.10.150.120. 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.
InterProIPR002888. 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]
PfamPF01315. 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]
PIRSFPIRSF000127. Xanthine_DH. 1 hit.
SMARTSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ8GUQ8.

Entry information

Entry nameXDH1_ARATH
AccessionPrimary (citable) accession number: Q8GUQ8
Secondary accession number(s): Q9SW46
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: March 1, 2003
Last modified: June 11, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names