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Reviewed, UniProtKB/Swiss-Prot O81796 (IDH3_ARATH)

Last modified November 25, 2008. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Isocitrate dehydrogenase [NAD] regulatory subunit 3, mitochondrial
    EC=1.1.1.41
Alternative name(s):
    Isocitric dehydrogenase 3
    NAD(+)-specific ICDH 3
    IDH-III
Gene names
Name: IDH3
Ordered Locus Names: At4g35650
ORF Names: F8D20.160
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length368 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Performs an essential role in the oxidative function of the citric acid cycle By similarity.

Catalytic activity

Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) + NADH.

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Subunit structure

Heteroligomer of catalytic and regulatory subunits.

Subcellular location

Mitochondrion.

Tissue specificity

Mainly expressed at a low level in pollen.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

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Ontologies

Keywords

   Biological processTricarboxylic acid cycle
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandMagnesium
Manganese
Metal-binding
NAD
   Molecular functionOxidoreductase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

tricarboxylic acid cycle

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrion

Inferred from electronic annotation. Source: InterPro

   Molecular functionisocitrate dehydrogenase (NAD+) activity

Inferred from electronic annotation. Source: InterPro

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2626Mitochondrion Potential
Chain27 – 368342Isocitrate dehydrogenase [NAD] regulatory subunit 3, mitochondrial
PRO_0000271289

Sites

Metal binding2351Magnesium or manganese By similarity
Binding site1171Substrate By similarity
Binding site1481Substrate By similarity
Binding site2351Substrate By similarity
Site1551Critical for catalysis By similarity
Site2021Critical for catalysis By similarity

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Sequences

Sequence LengthMass (Da)Tools
O81796-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 28EDD697B921650D

FASTA36839,957
        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

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References

« Hide 'large scale' references
[1]"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: 10617198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
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. expand/collapse author list , 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.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[3]"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
Plant Cell 16:241-256(2004) [PubMed: 14671022] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]"Characterization of a mutation in the IDH-II subunit of the NAD(+)-dependent isocitrate dehydrogenase from Arabidopsis thaliana."
Lin M., Behal R.H., Oliver D.J.
Plant Sci. 166:983-988(2004) [Agricola: IND43633651]
Cited for: GENE FAMILY.
[5]"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."
Lemaitre T., Hodges M.
Plant Cell Physiol. 47:634-643(2006) [PubMed: 16527867] [Abstract]
Cited for: TISSUE SPECIFICITY.

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Cross-references

Sequence databases

AL031135 Genomic DNA. Translation: CAA20035.1.
AL161587 Genomic DNA. Translation: CAB80281.1.
BT003922 mRNA. Translation: AAO41969.1.
BT006081 mRNA. Translation: AAP04066.1.
PIRT04670.
RefSeqNP_195290.1.
UniGeneAt.31403

3D structure databases

HSSPHSSP built from PDB template 1HQS based on UniProtKB P39126.
ModBaseSearch...

Genome annotation databases

GeneID829717.
GenomeReviewsGene locus AT4G35650 in contig CT486007_GR.
KEGGath:AT4G35650.
NMPDRfig|3702.1.peg.21650.

Organism-specific databases

GeneFarm4368. 439.
TAIRAt4g35650.

Family and domain databases

InterProIPR004434. IsoCit_DHase_NAD_mit.
IPR001804. IsoCit_IM_DHase.
[Graphical view]
Gene3DG3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHERPTHR11835. IDH_IMDH_dimeric. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR00175. mito_nad_idh. 1 hit.
PROSITEPS00470. IDH_IMDH. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameIDH3_ARATH
AccessionPrimary (citable) accession number: O81796
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1998
Last modified: November 25, 2008
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents