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)

P28834

- IDH1_YEAST

UniProt

P28834 - IDH1_YEAST

Protein

Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial

Gene

IDH1

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 127 (01 Oct 2014)
      Sequence version 2 (01 Jul 1993)
      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 sitei109 – 1091SubstrateBy similarity
    Binding sitei140 – 1401SubstrateBy similarity
    Sitei194 – 1941Critical for catalysisBy similarity
    Metal bindingi228 – 2281Magnesium or manganeseBy similarity
    Binding sitei228 – 2281SubstrateBy 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-13685.
    YEAST:YNL037C-MONOMER.
    ReactomeiREACT_189012. Mitochondrial protein import.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial (EC:1.1.1.41)
    Alternative name(s):
    Isocitric dehydrogenase
    NAD(+)-specific ICDH
    Gene namesi
    Name:IDH1
    Ordered Locus Names:YNL037C
    ORF Names:N2690
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIV

    Organism-specific databases

    CYGDiYNL037c.
    SGDiS000004982. IDH1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrial intermembrane space Source: Reactome
    3. mitochondrial isocitrate dehydrogenase complex (NAD+) Source: SGD
    4. mitochondrial matrix Source: SGD
    5. mitochondrial nucleoid Source: SGD

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1111Mitochondrion1 PublicationAdd
    BLAST
    Chaini12 – 360349Isocitrate dehydrogenase [NAD] subunit 1, mitochondrialPRO_0000014431Add
    BLAST

    Proteomic databases

    MaxQBiP28834.
    PaxDbiP28834.
    PeptideAtlasiP28834.

    Expressioni

    Gene expression databases

    GenevestigatoriP28834.

    Interactioni

    Subunit structurei

    Octamer of two non-identical subunits IDH1 and IDH2.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IDH2P282417EBI-8878,EBI-8883

    Protein-protein interaction databases

    BioGridi35787. 136 interactions.
    DIPiDIP-4376N.
    IntActiP28834. 6 interactions.
    MINTiMINT-484546.
    STRINGi4932.YNL037C.

    Structurei

    Secondary structure

    1
    360
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi29 – 379
    Helixi38 – 5316
    Beta strandi57 – 626
    Helixi71 – 8414
    Beta strandi85 – 917
    Helixi95 – 995
    Helixi102 – 1109
    Beta strandi114 – 1229
    Beta strandi135 – 1417
    Helixi145 – 1484
    Beta strandi150 – 1534
    Beta strandi158 – 1669
    Helixi167 – 18317
    Beta strandi188 – 1936
    Turni195 – 1973
    Helixi201 – 21616
    Beta strandi220 – 2267
    Helixi227 – 23610
    Helixi238 – 2403
    Beta strandi242 – 2465
    Helixi248 – 26215
    Helixi265 – 2673
    Beta strandi269 – 2768
    Beta strandi278 – 2803
    Turni283 – 2864
    Helixi289 – 2913
    Helixi300 – 31314
    Helixi317 – 33115
    Beta strandi332 – 3354
    Helixi338 – 3403
    Helixi346 – 35813

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BLVX-ray3.20A/C/E/G12-360[»]
    3BLWX-ray4.30A/C/E/G/I/K/M/O12-360[»]
    3BLXX-ray2.70A/C/E/G/I/K/M/O12-360[»]
    ProteinModelPortaliP28834.
    SMRiP28834. Positions 28-360.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28834.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0473.
    GeneTreeiENSGT00590000083091.
    HOGENOMiHOG000021113.
    KOiK00030.
    OMAiMASCDAT.
    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.

    P28834-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLNRTIAKRT LATAAQAERT LPKKYGGRFT VTLIPGDGVG KEITDSVRTI    50
    FEAENIPIDW ETINIKQTDH KEGVYEAVES LKRNKIGLKG LWHTPADQTG 100
    HGSLNVALRK QLDIYANVAL FKSLKGVKTR IPDIDLIVIR ENTEGEFSGL 150
    EHESVPGVVE SLKVMTRPKT ERIARFAFDF AKKYNRKSVT AVHKANIMKL 200
    GDGLFRNIIT EIGQKEYPDI DVSSIIVDNA SMQAVAKPHQ FDVLVTPSMY 250
    GTILGNIGAA LIGGPGLVAG ANFGRDYAVF EPGSRHVGLD IKGQNVANPT 300
    AMILSSTLML NHLGLNEYAT RISKAVHETI AEGKHTTRDI GGSSSTTDFT 350
    NEIINKLSTM 360
    Length:360
    Mass (Da):39,324
    Last modified:July 1, 1993 - v2
    Checksum:i0932E7B3CD685240
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95203 Genomic DNA. Translation: AAA34711.1.
    Z71313 Genomic DNA. Translation: CAA95904.1.
    BK006947 Genomic DNA. Translation: DAA10508.1.
    PIRiS31264.
    RefSeqiNP_014361.1. NM_001182876.1.

    Genome annotation databases

    EnsemblFungiiYNL037C; YNL037C; YNL037C.
    GeneIDi855691.
    KEGGisce:YNL037C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95203 Genomic DNA. Translation: AAA34711.1 .
    Z71313 Genomic DNA. Translation: CAA95904.1 .
    BK006947 Genomic DNA. Translation: DAA10508.1 .
    PIRi S31264.
    RefSeqi NP_014361.1. NM_001182876.1.

    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 A/C/E/G 12-360 [» ]
    3BLW X-ray 4.30 A/C/E/G/I/K/M/O 12-360 [» ]
    3BLX X-ray 2.70 A/C/E/G/I/K/M/O 12-360 [» ]
    ProteinModelPortali P28834.
    SMRi P28834. Positions 28-360.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35787. 136 interactions.
    DIPi DIP-4376N.
    IntActi P28834. 6 interactions.
    MINTi MINT-484546.
    STRINGi 4932.YNL037C.

    Proteomic databases

    MaxQBi P28834.
    PaxDbi P28834.
    PeptideAtlasi P28834.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YNL037C ; YNL037C ; YNL037C .
    GeneIDi 855691.
    KEGGi sce:YNL037C.

    Organism-specific databases

    CYGDi YNL037c.
    SGDi S000004982. IDH1.

    Phylogenomic databases

    eggNOGi COG0473.
    GeneTreei ENSGT00590000083091.
    HOGENOMi HOG000021113.
    KOi K00030.
    OMAi MASCDAT.
    OrthoDBi EOG75XGWZ.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-13685.
    YEAST:YNL037C-MONOMER.
    Reactomei REACT_189012. Mitochondrial protein import.

    Miscellaneous databases

    EvolutionaryTracei P28834.
    NextBioi 980007.
    PROi P28834.

    Gene expression databases

    Genevestigatori P28834.

    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. "Cloning and characterization of the gene encoding the IDH1 subunit of NAD(+)-dependent isocitrate dehydrogenase from Saccharomyces cerevisiae."
      Cupp J.R., McAlister-Henn L.
      J. Biol. Chem. 267:16417-16423(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 49-61; 72-83; 325-333 AND 339-356.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "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 12-27.
      Strain: SG7.
    5. "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.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiIDH1_YEAST
    AccessioniPrimary (citable) accession number: P28834
    Secondary accession number(s): D6W1E2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 10500 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 XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

    External Data

    Dasty 3