Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O81796

- IDH3_ARATH

UniProt

O81796 - IDH3_ARATH

Protein

Isocitrate dehydrogenase [NAD] regulatory subunit 3, mitochondrial

Gene

IDH3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Binds 1 magnesium or manganese 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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, NAD

    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

    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.

    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.
    OMAiMASCDAT.
    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

    MARRSVSIFN RLLANPPSPF TSLSRSITYM PRPGDGAPRT VTLIPGDGIG    50
    PLVTGAVEQV MEAMHAPVHF ERYEVLGNMR KVPEEVIESV KRNKVCLKGG 100
    LATPVGGGVS SLNMQLRKEL DIFASLVNCI NVPGLVTRHE NVDIVVIREN 150
    TEGEYSGLEH EVVPGVVESL KVITKFCSER IARYAFEYAY LNNRKKVTAV 200
    HKANIMKLAD GLFLESCREV AKHYSGITYN EIIVDNCCMQ LVAKPEQFDV 250
    MVTPNLYGNL IANTAAGIAG GTGVMPGGNV GAEHAIFEQG ASAGNVGNDK 300
    MVEQKKANPV ALLLSSAMML RHLRFPTFAD RLETAVKQVI KEGKYRTKDL 350
    GGDCTTQEVV DAVIAALE 368
    Length:368
    Mass (Da):39,957
    Last modified:November 1, 1998 - v1
    Checksum:i28EDD697B921650D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi T04670.
    RefSeqi NP_195290.1. NM_119730.2.
    UniGenei At.31403.

    3D structure databases

    ProteinModelPortali O81796.
    SMRi O81796. Positions 36-367.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 14999. 3 interactions.
    MINTi MINT-8061753.
    STRINGi 3702.AT4G35650.1-P.

    Proteomic databases

    PaxDbi O81796.
    PRIDEi O81796.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G35650.1 ; AT4G35650.1 ; AT4G35650 .
    GeneIDi 829717.
    KEGGi ath:AT4G35650.

    Organism-specific databases

    GeneFarmi 4368. 439.
    TAIRi AT4G35650.

    Phylogenomic databases

    eggNOGi COG0473.
    HOGENOMi HOG000021113.
    InParanoidi O81796.
    KOi K00030.
    OMAi MASCDAT.
    PhylomeDBi O81796.

    Gene expression databases

    Genevestigatori O81796.

    Family and domain databases

    Gene3Di 3.40.718.10. 1 hit.
    InterProi IPR001804. Isocitrate/isopropylmalate_DH.
    IPR004434. Isocitrate_DH_NAD.
    IPR024084. IsoPropMal-DH-like_dom.
    [Graphical view ]
    PANTHERi PTHR11835. PTHR11835. 1 hit.
    Pfami PF00180. Iso_dh. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00175. mito_nad_idh. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.

    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: October 1, 2014
    This is version 94 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