ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry O81796


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name IDH3_ARATH
Primary accession number O81796
Secondary accession numbers None
Integrated into Swiss-Prot on January 9, 2007
Sequence was last modified on November 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 47)
Name and origin of the protein
Protein name Isocitrate dehydrogenase [NAD] regulatory subunit 3, mitochondrial [Precursor]
Synonyms EC 1.1.1.41
Isocitric dehydrogenase 3
NAD(+)-specific ICDH 3
IDH-III
Gene name
Name: IDH3
OrderedLocusNames: At4g35650
ORFNames: F8D20.160
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1105/tpc.016055; PubMed=14671022 [NCBI, ExPASy, EBI, Israel, Japan]
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.;
"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins.";
Plant Cell 16:241-256(2004).
[4]
GENE FAMILY.
DOI=10.1016/j.plantsci.2003.12.012; AGRICOLA=IND43633651
Lin M., Behal R.H., Oliver D.J.;
"Characterization of a mutation in the IDH-II subunit of the NAD(+)-dependent isocitrate dehydrogenase from Arabidopsis thaliana.";
Plant Sci. 166:983-988(2004).
[5]
TISSUE SPECIFICITY.
DOI=10.1093/pcp/pcj030; PubMed=16527867 [NCBI, ExPASy, EBI, Israel, Japan]
Lemaitre T., Hodges M.;
"Expression analysis of Arabidopsis thaliana NAD-dependent isocitrate dehydrogenase genes shows the presence of a functional subunit that is mainly expressed in the pollen and absent from vegetative organs.";
Plant Cell Physiol. 47:634-643(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AL031135; CAA20035.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161587; CAB80281.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT003922; AAO41969.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006081; AAP04066.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T04670; T04670.
RefSeq NP_195290.1; -.
UniGene At.31403
3D structure databases
HSSP P39126; 1HQS. [HSSP ENTRY / PDB]
ModBase O81796.
Organism-specific databases
GeneFarm 4368; 439.
TAIR At4g35650; -.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from InterPro).
GO:0004449; Molecular function: isocitrate dehydrogenase (NAD+) activity (inferred from electronic annotation from InterPro).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145; Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006099; Biological process: tricarboxylic acid cycle (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR004434; IsoCit_DHase_NAD_mit.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.718.10; IDH_IMDH; 1.
PANTHER PTHR11835; IDH_IMDH_dimeric; 1.
Pfam PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00175; mito_nad_idh; 1.
PROSITE PS00470; IDH_IMDH; FALSE_NEG.
Genome annotation databases
GeneID 829717; -.
GenomeReviews CT486007_GR; AT4G35650.
KEGG ath:AT4G35650; -.
NMPDR fig|3702.1.peg.21650; -.
Other
ProtoNet O81796.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Magnesium; Manganese; Metal-binding; Mitochondrion; NAD; Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    26  26     Mitochondrion (Potential). 
CHAIN   27   368  342     Isocitrate dehydrogenase [NAD] regulatory subunit 3, mitochondrial. PRO_0000271289
METAL   235   235        Magnesium or manganese (By similarity). 
BINDING   117   117        Substrate (By similarity). 
BINDING   148   148        Substrate (By similarity). 
BINDING   235   235        Substrate (By similarity). 
SITE   155   155  1     Critical for catalysis (By similarity). 
SITE   202   202  1     Critical for catalysis (By similarity). 
Sequence information
Length: 368 AA [This is the length of the unprocessed precursor] Molecular weight: 39957 Da [This is the MW of the unprocessed precursor] CRC64: 28EDD697B921650D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MARRSVSIFN RLLANPPSPF TSLSRSITYM PRPGDGAPRT VTLIPGDGIG PLVTGAVEQV 

        70         80         90        100        110        120 
MEAMHAPVHF ERYEVLGNMR KVPEEVIESV KRNKVCLKGG LATPVGGGVS SLNMQLRKEL 

       130        140        150        160        170        180 
DIFASLVNCI NVPGLVTRHE NVDIVVIREN TEGEYSGLEH EVVPGVVESL KVITKFCSER 

       190        200        210        220        230        240 
IARYAFEYAY LNNRKKVTAV HKANIMKLAD GLFLESCREV AKHYSGITYN EIIVDNCCMQ 

       250        260        270        280        290        300 
LVAKPEQFDV MVTPNLYGNL IANTAAGIAG GTGVMPGGNV GAEHAIFEQG ASAGNVGNDK 

       310        320        330        340        350        360 
MVEQKKANPV ALLLSSAMML RHLRFPTFAD RLETAVKQVI KEGKYRTKDL GGDCTTQEVV 


DAVIAALE 

O81796 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by kr flag YPRC Korea Mirror sites: Australia  Brazil  Canada  China  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!