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Protein

Isocitrate dehydrogenase [NAD] regulatory subunit 3, mitochondrial

Gene

IDH3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH.

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 1 Mg(2+) or Mn2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei117 – 1171SubstrateBy similarity
Binding sitei148 – 1481SubstrateBy similarity
Sitei155 – 1551Critical for catalysisBy similarity
Sitei202 – 2021Critical for catalysisBy similarity
Metal bindingi235 – 2351Magnesium or manganeseBy similarity
Binding sitei235 – 2351SubstrateBy similarity

GO - Molecular functioni

  1. isocitrate dehydrogenase (NAD+) activity Source: TAIR
  2. magnesium ion binding Source: InterPro
  3. NAD binding Source: InterPro

GO - Biological processi

  1. isocitrate metabolic process Source: TAIR
  2. tricarboxylic acid cycle Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, NAD

Enzyme and pathway databases

ReactomeiREACT_242439. Citric acid cycle (TCA cycle).

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate dehydrogenase [NAD] regulatory subunit 3, mitochondrial (EC:1.1.1.41)
Alternative name(s):
IDH-III
Isocitric dehydrogenase 3
NAD(+)-specific ICDH 3
Gene namesi
Name:IDH3
Ordered Locus Names:At4g35650
ORF Names:F8D20.160
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G35650.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. apoplast Source: TAIR
  2. mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2626MitochondrionSequence AnalysisAdd
BLAST
Chaini27 – 368342Isocitrate dehydrogenase [NAD] regulatory subunit 3, mitochondrialPRO_0000271289Add
BLAST

Proteomic databases

PaxDbiO81796.
PRIDEiO81796.

Expressioni

Tissue specificityi

Mainly expressed at a low level in pollen.1 Publication

Gene expression databases

GenevestigatoriO81796.

Interactioni

Subunit structurei

Heterooligomer of catalytic and regulatory subunits. Interacts with 14-3-3-like proteins GRF1 GRF3 and GRF8 (PubMed:22104211).1 Publication

Protein-protein interaction databases

BioGridi14999. 3 interactions.
MINTiMINT-8061753.
STRINGi3702.AT4G35650.1-P.

Structurei

3D structure databases

ProteinModelPortaliO81796.
SMRiO81796. Positions 36-367.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0473.
HOGENOMiHOG000021113.
InParanoidiO81796.
KOiK00030.
OMAiREVAKHY.
PhylomeDBiO81796.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
InterProiIPR001804. Isocitrate/isopropylmalate_DH.
IPR004434. Isocitrate_DH_NAD.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERiPTHR11835. PTHR11835. 1 hit.
PfamiPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00175. mito_nad_idh. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O81796-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARRSVSIFN RLLANPPSPF TSLSRSITYM PRPGDGAPRT VTLIPGDGIG
60 70 80 90 100
PLVTGAVEQV MEAMHAPVHF ERYEVLGNMR KVPEEVIESV KRNKVCLKGG
110 120 130 140 150
LATPVGGGVS SLNMQLRKEL DIFASLVNCI NVPGLVTRHE NVDIVVIREN
160 170 180 190 200
TEGEYSGLEH EVVPGVVESL KVITKFCSER IARYAFEYAY LNNRKKVTAV
210 220 230 240 250
HKANIMKLAD GLFLESCREV AKHYSGITYN EIIVDNCCMQ LVAKPEQFDV
260 270 280 290 300
MVTPNLYGNL IANTAAGIAG GTGVMPGGNV GAEHAIFEQG ASAGNVGNDK
310 320 330 340 350
MVEQKKANPV ALLLSSAMML RHLRFPTFAD RLETAVKQVI KEGKYRTKDL
360
GGDCTTQEVV DAVIAALE
Length:368
Mass (Da):39,957
Last modified:November 1, 1998 - v1
Checksum:i28EDD697B921650D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL031135 Genomic DNA. Translation: CAA20035.1.
AL161587 Genomic DNA. Translation: CAB80281.1.
CP002687 Genomic DNA. Translation: AEE86544.1.
BT003922 mRNA. Translation: AAO41969.1.
BT006081 mRNA. Translation: AAP04066.1.
PIRiT04670.
RefSeqiNP_195290.1. NM_119730.2.
UniGeneiAt.31403.

Genome annotation databases

EnsemblPlantsiAT4G35650.1; AT4G35650.1; AT4G35650.
GeneIDi829717.
KEGGiath:AT4G35650.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL031135 Genomic DNA. Translation: CAA20035.1.
AL161587 Genomic DNA. Translation: CAB80281.1.
CP002687 Genomic DNA. Translation: AEE86544.1.
BT003922 mRNA. Translation: AAO41969.1.
BT006081 mRNA. Translation: AAP04066.1.
PIRiT04670.
RefSeqiNP_195290.1. NM_119730.2.
UniGeneiAt.31403.

3D structure databases

ProteinModelPortaliO81796.
SMRiO81796. Positions 36-367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14999. 3 interactions.
MINTiMINT-8061753.
STRINGi3702.AT4G35650.1-P.

Proteomic databases

PaxDbiO81796.
PRIDEiO81796.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G35650.1; AT4G35650.1; AT4G35650.
GeneIDi829717.
KEGGiath:AT4G35650.

Organism-specific databases

GeneFarmi4368. 439.
TAIRiAT4G35650.

Phylogenomic databases

eggNOGiCOG0473.
HOGENOMiHOG000021113.
InParanoidiO81796.
KOiK00030.
OMAiREVAKHY.
PhylomeDBiO81796.

Enzyme and pathway databases

ReactomeiREACT_242439. Citric acid cycle (TCA cycle).

Gene expression databases

GenevestigatoriO81796.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
InterProiIPR001804. Isocitrate/isopropylmalate_DH.
IPR004434. Isocitrate_DH_NAD.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERiPTHR11835. PTHR11835. 1 hit.
PfamiPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00175. mito_nad_idh. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Landsberg erecta.
  5. "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] [Europe PMC]
    Cited for: GENE FAMILY.
  6. "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] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "Determining novel functions of Arabidopsis 14-3-3 proteins in central metabolic processes."
    Diaz C., Kusano M., Sulpice R., Araki M., Redestig H., Saito K., Stitt M., Shin R.
    BMC Syst. Biol. 5:192-192(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GRF1; GRF3 AND GRF8.

Entry informationi

Entry nameiIDH3_ARATH
AccessioniPrimary (citable) accession number: O81796
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1998
Last modified: January 7, 2015
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.