Q8GUQ8 (XDH1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Xanthine dehydrogenase 1
Short name=AtXDH1
EC=1.17.1.4

Gene names

Name:	XDH1
Ordered Locus Names:	At4g34890
ORF Names:	T11I11.130

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	1361 AA.
Sequence status	Complete.
Protein existence	Evidence 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 ion (molybdopterin) 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.

Ontologies

Keywords
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	purine nucleobase catabolic process Inferred from mutant phenotype Ref.6. Source: TAIR response to reactive oxygen species Inferred from mutant phenotype Ref.7. Source: TAIR response to water deprivation Inferred from mutant phenotype Ref.7. Source: TAIR superoxide anion generation Inferred from mutant phenotype Ref.4. Source: TAIR xanthine metabolic process Inferred from mutant phenotype Ref.5. Source: TAIR
Cellular_component	cytosol Inferred from direct assay PubMed 21166475. Source: TAIR
Molecular_function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW UDP-N-acetylmuramate dehydrogenase activity Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro xanthine dehydrogenase activity Inferred from direct assay Ref.1. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1361	1361	Xanthine dehydrogenase 1		PRO_0000417457
Regions
	Domain	15 – 101	87	2Fe-2S ferredoxin-type
	Domain	257 – 442	186	FAD-binding PCMH-type
	Nucleotide binding	285 – 292	8	FAD By similarity
	Nucleotide binding	375 – 379	5	FAD By similarity
Sites
	Active site	1297	1	Proton acceptor By similarity
	Metal binding	53	1	Iron-sulfur (2Fe-2S) 1 By similarity
	Metal binding	58	1	Iron-sulfur (2Fe-2S) 1 By similarity
	Metal binding	61	1	Iron-sulfur (2Fe-2S) 1 By similarity
	Metal binding	83	1	Iron-sulfur (2Fe-2S) 1 By similarity
	Metal binding	123	1	Iron-sulfur (2Fe-2S) 2 By similarity
	Metal binding	126	1	Iron-sulfur (2Fe-2S) 2 By similarity
	Metal binding	159	1	Iron-sulfur (2Fe-2S) 2 By similarity
	Metal binding	161	1	Iron-sulfur (2Fe-2S) 2 By similarity
	Metal binding	796	1	Molybdenum By similarity
	Metal binding	827	1	Molybdenum; via carbonyl oxygen By similarity
	Metal binding	941	1	Molybdenum; via amide nitrogen By similarity
	Metal binding	1108	1	Molybdenum; via amide nitrogen By similarity
	Binding site	365	1	FAD By similarity
	Binding site	388	1	FAD By similarity
	Binding site	432	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	450	1	FAD By similarity
	Binding site	831	1	Substrate By similarity
	Binding site	909	1	Substrate By similarity
	Binding site	943	1	Substrate By similarity
	Binding site	1039	1	Substrate By similarity
Experimental info
	Mutagenesis	364	1	W → A: Decreases activity 8-fold. Ref.8
	Mutagenesis	421	1	Y → A: Decreases activity 4-fold. Ref.8
	Mutagenesis	831	1	E → A: Loss of activity. Ref.8
	Mutagenesis	909	1	R → A: Decreases activity 12-fold. Ref.8
	Mutagenesis	1297	1	E → A: Decreases activity 40-fold. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Q8GUQ8 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: BF72FE23A1D59C88	FASTA	1,361	149,196
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00529753.
PIR	T10235.
RefSeq	NP_195215.2. NM_119655.3.
UniGene	At.27839.
3D structure databases
HSSP	HSSP built from PDB template 1FO4 based on UniProtKB P80457.
ProteinModelPortal	Q8GUQ8.
SMR	Q8GUQ8. Positions 16-176, 238-553, 597-1347.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT4G34890.1-P.
Proteomic databases
PaxDb	Q8GUQ8.
PRIDE	Q8GUQ8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G34890.1; AT4G34890.1; AT4G34890.
GeneID	829641.
KEGG	ath:AT4G34890.
Organism-specific databases
TAIR	At4g34890.
Phylogenomic databases
eggNOG	COG4630.
HOGENOM	HOG000191197.
InParanoid	Q8GUQ8.
KO	K00106.
OMA	VASCNED.
PhylomeDB	Q8GUQ8.
ProtClustDB	PLN02906.
Enzyme and pathway databases
BioCyc	ARA:AT4G34890-MONOMER. MetaCyc:AT4G34890-MONOMER.
BRENDA	1.17.1.4. 302.
Gene expression databases
ArrayExpress	Q8GUQ8.
Genevestigator	Q8GUQ8.
Family and domain databases
Gene3D	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.
InterPro	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]
Pfam	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]
PIRSF	PIRSF000127. Xanthine_DH. 1 hit.
SMART	SM01008. Ald_Xan_dh_C. 1 hit. SM01092. CO_deh_flav_C. 1 hit. [Graphical view]
SUPFAM	SSF47741. 2Fe-2S_bind. 1 hit. SSF56003. Ald_xan_DH_mo_bd. 1 hit. SSF54665. Aldxan_dh_hamm. 1 hit. SSF55447. CO_deh_flav_C. 1 hit. SSF56176. FAD-binding_2. 1 hit. SSF54292. Ferredoxin. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51387. FAD_PCMH. 1 hit. PS00559. MOLYBDOPTERIN_EUK. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XDH1_ARATH

Accession

Primary (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:	May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program