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Q8GUQ8

- XDH1_ARATH

UniProt

Q8GUQ8 - XDH1_ARATH

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Protein

Xanthine dehydrogenase 1

Gene
XDH1, At4g34890, T11I11.130
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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

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) 1 By similarity
Metal bindingi58 – 581Iron-sulfur (2Fe-2S) 1 By similarity
Metal bindingi61 – 611Iron-sulfur (2Fe-2S) 1 By similarity
Metal bindingi83 – 831Iron-sulfur (2Fe-2S) 1 By similarity
Metal bindingi123 – 1231Iron-sulfur (2Fe-2S) 2 By similarity
Metal bindingi126 – 1261Iron-sulfur (2Fe-2S) 2 By similarity
Metal bindingi159 – 1591Iron-sulfur (2Fe-2S) 2 By similarity
Metal bindingi161 – 1611Iron-sulfur (2Fe-2S) 2 By similarity
Binding sitei365 – 3651FAD By similarity
Binding sitei388 – 3881FAD By similarity
Binding sitei432 – 4321FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei450 – 4501FAD By similarity
Metal bindingi796 – 7961Molybdenum By similarity
Metal bindingi827 – 8271Molybdenum; via carbonyl oxygen By similarity
Binding sitei831 – 8311Substrate By similarity
Binding sitei909 – 9091Substrate By similarity
Metal bindingi941 – 9411Molybdenum; via amide nitrogen By similarity
Binding sitei943 – 9431Substrate By similarity
Binding sitei1039 – 10391Substrate By similarity
Metal bindingi1108 – 11081Molybdenum; via amide nitrogen By similarity
Active sitei1297 – 12971Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi285 – 2928FAD By similarity
Nucleotide bindingi375 – 3795FAD By 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
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. 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
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 Inferred.1 Publication

Protein-protein interaction databases

STRINGi3702.AT4G34890.1-P.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 101872Fe-2S ferredoxin-typeAdd
BLAST
Domaini257 – 442186FAD-binding PCMH-typeAdd
BLAST

Sequence similaritiesi

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

« 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(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: September 3, 2014
This is version 88 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