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)

P28241

- IDH2_YEAST

UniProt

P28241 - IDH2_YEAST

Protein

Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial

Gene

IDH2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Performs an essential role in the oxidative function of the citric acid cycle. Also binds RNA; specifically to the 5'-untranslated leaders of mitochondrial mRNAs.

    Catalytic activityi

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

    Cofactori

    Binds 1 magnesium or manganese ion per subunit.By similarity

    Enzyme regulationi

    Allosterically regulated by several compounds including AMP, NAD+, and citrate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei119 – 1191SubstrateBy similarity
    Binding sitei129 – 1291SubstrateBy similarity
    Binding sitei150 – 1501SubstrateBy similarity
    Sitei157 – 1571Critical for catalysisBy similarity
    Sitei204 – 2041Critical for catalysisBy similarity
    Metal bindingi237 – 2371Magnesium or manganeseBy similarity
    Binding sitei237 – 2371SubstrateBy similarity
    Metal bindingi263 – 2631Magnesium or manganeseBy similarity
    Metal bindingi267 – 2671Magnesium or manganeseBy similarity

    GO - Molecular functioni

    1. isocitrate dehydrogenase (NAD+) activity Source: UniProtKB-EC
    2. magnesium ion binding Source: InterPro
    3. NAD binding Source: InterPro
    4. protein binding Source: IntAct
    5. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. glutamate biosynthetic process Source: SGD
    2. isocitrate metabolic process Source: SGD
    3. tricarboxylic acid cycle Source: SGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, NAD, RNA-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13686.
    YEAST:YOR136W-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial (EC:1.1.1.41)
    Alternative name(s):
    Isocitric dehydrogenase
    NAD(+)-specific ICDH
    Gene namesi
    Name:IDH2
    Ordered Locus Names:YOR136W
    ORF Names:O3326, YOR3326W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOR136w.
    SGDiS000005662. IDH2.

    Subcellular locationi

    Mitochondrion matrix 1 Publication

    GO - Cellular componenti

    1. mitochondrial isocitrate dehydrogenase complex (NAD+) Source: SGD
    2. mitochondrion Source: SGD

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1515Mitochondrion2 PublicationsAdd
    BLAST
    Chaini16 – 369354Isocitrate dehydrogenase [NAD] subunit 2, mitochondrialPRO_0000014434Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei105 – 1051Phosphothreonine1 Publication
    Modified residuei153 – 1531Phosphothreonine2 Publications
    Modified residuei327 – 3271Phosphothreonine1 Publication
    Modified residuei349 – 3491Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP28241.
    PaxDbiP28241.
    PeptideAtlasiP28241.

    Expressioni

    Gene expression databases

    GenevestigatoriP28241.

    Interactioni

    Subunit structurei

    Octamer of two non-identical subunits IDH1 and IDH2.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IDH1P288347EBI-8883,EBI-8878

    Protein-protein interaction databases

    BioGridi34531. 171 interactions.
    DIPiDIP-4296N.
    IntActiP28241. 25 interactions.
    MINTiMINT-559185.
    STRINGi4932.YOR136W.

    Structurei

    Secondary structure

    1
    369
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 243
    Turni32 – 343
    Helixi48 – 6013
    Turni61 – 633
    Beta strandi65 – 673
    Beta strandi76 – 783
    Beta strandi81 – 833
    Helixi86 – 9510
    Beta strandi96 – 1005
    Helixi114 – 1229
    Beta strandi124 – 1329
    Beta strandi145 – 1517
    Beta strandi153 – 16311
    Beta strandi168 – 1769
    Helixi177 – 19317
    Beta strandi197 – 2048
    Turni206 – 2083
    Helixi210 – 22314
    Beta strandi229 – 2357
    Helixi236 – 24510
    Helixi247 – 2504
    Beta strandi253 – 2575
    Helixi259 – 27315
    Helixi277 – 2793
    Beta strandi281 – 2888
    Beta strandi290 – 2945
    Helixi300 – 3023
    Turni303 – 3064
    Helixi311 – 32414
    Helixi327 – 3359
    Helixi337 – 3415
    Helixi350 – 3523
    Helixi358 – 36710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BLVX-ray3.20B/D/F/H16-369[»]
    3BLWX-ray4.30B/D/F/H/J/L/N/P16-369[»]
    3BLXX-ray2.70B/D/F/H/J/L/N/P16-369[»]
    ProteinModelPortaliP28241.
    SMRiP28241. Positions 19-369.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28241.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0473.
    GeneTreeiENSGT00550000074918.
    HOGENOMiHOG000021113.
    KOiK00030.
    OMAiTPIAWEP.
    OrthoDBiEOG75XGWZ.

    Family and domain databases

    Gene3Di3.40.718.10. 1 hit.
    InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
    IPR001804. 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.
    PROSITEiPS00470. IDH_IMDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P28241-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRNTFFRNT SRRFLATVKQ PSIGRYTGKP NPSTGKYTVS FIEGDGIGPE    50
    ISKSVKKIFS AANVPIEWES CDVSPIFVNG LTTIPDPAVQ SITKNLVALK 100
    GPLATPIGKG HRSLNLTLRK TFGLFANVRP AKSIEGFKTT YENVDLVLIR 150
    ENTEGEYSGI EHIVCPGVVQ SIKLITRDAS ERVIRYAFEY ARAIGRPRVI 200
    VVHKSTIQRL ADGLFVNVAK ELSKEYPDLT LETELIDNSV LKVVTNPSAY 250
    TDAVSVCPNL YGDILSDLNS GLSAGSLGLT PSANIGHKIS IFEAVHGSAP 300
    DIAGQDKANP TALLLSSVMM LNHMGLTNHA DQIQNAVLST IASGPENRTG 350
    DLAGTATTSS FTEAVIKRL 369
    Length:369
    Mass (Da):39,739
    Last modified:December 1, 1992 - v1
    Checksum:i3A48C999776CE373
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251R → G AA sequence (PubMed:2198251)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74131 Genomic DNA. Translation: AAA34702.1.
    X94335 Genomic DNA. Translation: CAA64054.1.
    Z75043 Genomic DNA. Translation: CAA99335.1.
    X90518 Genomic DNA. Translation: CAA62110.1.
    BK006948 Genomic DNA. Translation: DAA10909.1.
    PIRiA39309.
    RefSeqiNP_014779.1. NM_001183555.1.

    Genome annotation databases

    EnsemblFungiiYOR136W; YOR136W; YOR136W.
    GeneIDi854303.
    KEGGisce:YOR136W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74131 Genomic DNA. Translation: AAA34702.1 .
    X94335 Genomic DNA. Translation: CAA64054.1 .
    Z75043 Genomic DNA. Translation: CAA99335.1 .
    X90518 Genomic DNA. Translation: CAA62110.1 .
    BK006948 Genomic DNA. Translation: DAA10909.1 .
    PIRi A39309.
    RefSeqi NP_014779.1. NM_001183555.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BLV X-ray 3.20 B/D/F/H 16-369 [» ]
    3BLW X-ray 4.30 B/D/F/H/J/L/N/P 16-369 [» ]
    3BLX X-ray 2.70 B/D/F/H/J/L/N/P 16-369 [» ]
    ProteinModelPortali P28241.
    SMRi P28241. Positions 19-369.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34531. 171 interactions.
    DIPi DIP-4296N.
    IntActi P28241. 25 interactions.
    MINTi MINT-559185.
    STRINGi 4932.YOR136W.

    Proteomic databases

    MaxQBi P28241.
    PaxDbi P28241.
    PeptideAtlasi P28241.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOR136W ; YOR136W ; YOR136W .
    GeneIDi 854303.
    KEGGi sce:YOR136W.

    Organism-specific databases

    CYGDi YOR136w.
    SGDi S000005662. IDH2.

    Phylogenomic databases

    eggNOGi COG0473.
    GeneTreei ENSGT00550000074918.
    HOGENOMi HOG000021113.
    KOi K00030.
    OMAi TPIAWEP.
    OrthoDBi EOG75XGWZ.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-13686.
    YEAST:YOR136W-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P28241.
    NextBioi 976313.
    PROi P28241.

    Gene expression databases

    Genevestigatori P28241.

    Family and domain databases

    Gene3Di 3.40.718.10. 1 hit.
    InterProi IPR019818. IsoCit/isopropylmalate_DH_CS.
    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.
    PROSITEi PS00470. IDH_IMDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "NAD(+)-dependent isocitrate dehydrogenase. Cloning, nucleotide sequence, and disruption of the IDH2 gene from Saccharomyces cerevisiae."
      Cupp J.R., McAlister-Henn L.
      J. Biol. Chem. 266:22199-22205(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Sequencing and analysis of 51 kb on the right arm of chromosome XV from Saccharomyces cerevisiae reveals 30 open reading frames."
      Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C., Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.
      Yeast 12:281-288(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. "Subunit structure, expression, and function of NAD(H)-specific isocitrate dehydrogenase in Saccharomyces cerevisiae."
      Keys D.A., McAlister-Henn L.
      J. Bacteriol. 172:4280-4287(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 16-26.
      Strain: SG7.
    7. "Yeast mitochondrial NAD(+)-dependent isocitrate dehydrogenase is an RNA-binding protein."
      Elzinga S.D.J., Bednarz A.L., van Oosterum K., Dekker P.J.T., Grivell L.A.
      Nucleic Acids Res. 21:5328-5331(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING, PROTEIN SEQUENCE OF 16-34.
    8. "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."
      Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.
      Biochemistry 40:9758-9769(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
      Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
      Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.
    11. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-105 AND THR-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-153 AND THR-327, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiIDH2_YEAST
    AccessioniPrimary (citable) accession number: P28241
    Secondary accession number(s): D6W2J3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 136 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 43100 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3