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P33198

- IDHP_PIG

UniProt

P33198 - IDHP_PIG

Protein

Isocitrate dehydrogenase [NADP], mitochondrial

Gene

IDH2

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    Functioni

    Plays a role in intermediary metabolism and energy production. It may tightly associate or interact with the pyruvate dehydrogenase complex.

    Catalytic activityi

    Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH.

    Cofactori

    Binds 1 magnesium or manganese ion per subunit.

    Kineticsi

    1. KM=7.47 µM for isocitrate
    2. KM=9.85 µM for NADP
    3. KM=0.11 µM for manganese

    Vmax=39.6 µmol/min/mg enzyme with isocitrate as substrate

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei86 – 861Substrate
    Binding sitei91 – 911NADPBy similarity
    Binding sitei118 – 1181Substrate
    Binding sitei141 – 1411Substrate
    Sitei148 – 1481Critical for catalysis
    Sitei220 – 2201Critical for catalysis
    Metal bindingi260 – 2601Magnesium or manganese
    Binding sitei268 – 2681NADPBy similarity
    Metal bindingi283 – 2831Magnesium or manganese
    Binding sitei336 – 3361NADP; via amide nitrogen and carbonyl oxygen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi84 – 863NADPBy similarity
    Nucleotide bindingi318 – 3236NADPBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: UniProtKB
    2. glyoxylate cycle Source: UniProtKB-KW
    3. isocitrate metabolic process Source: UniProtKB
    4. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glyoxylate bypass, Tricarboxylic acid cycle

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, NADP

    Enzyme and pathway databases

    ReactomeiREACT_217226. Citric acid cycle (TCA cycle).
    SABIO-RKP33198.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isocitrate dehydrogenase [NADP], mitochondrial (EC:1.1.1.42)
    Short name:
    IDH
    Alternative name(s):
    ICD-M
    IDP
    NADP(+)-specific ICDH
    Oxalosuccinate decarboxylase
    Gene namesi
    Name:IDH2
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: Ensembl

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi148 – 1481Y → F: Large decrease in Vmax and insignificant change in KM for isocitrate and NADP. 1 Publication
    Mutagenesisi220 – 2201K → Q or Y: Large decrease in Vmax and insignificant change in KM for isocitrate and NADP. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei‹1 – 8›8Mitochondrion
    Chaini9 – 421413Isocitrate dehydrogenase [NADP], mitochondrialPRO_0000014422Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei14 – 141N6-acetyllysineBy similarity
    Modified residuei17 – 171N6-acetyllysineBy similarity
    Modified residuei36 – 361N6-acetyllysineBy similarity
    Modified residuei38 – 381N6-acetyllysineBy similarity
    Modified residuei49 – 491N6-acetyllysine; alternateBy similarity
    Modified residuei49 – 491N6-succinyllysine; alternateBy similarity
    Modified residuei75 – 751N6-acetyllysine; alternateBy similarity
    Modified residuei75 – 751N6-succinyllysine; alternateBy similarity
    Modified residuei124 – 1241N6-acetyllysineBy similarity
    Modified residuei135 – 1351N6-acetyllysine; alternateBy similarity
    Modified residuei135 – 1351N6-succinyllysine; alternateBy similarity
    Modified residuei149 – 1491N6-acetyllysine; alternateBy similarity
    Modified residuei149 – 1491N6-succinyllysine; alternateBy similarity
    Modified residuei162 – 1621N6-acetyllysine; alternateBy similarity
    Modified residuei162 – 1621N6-succinyllysine; alternateBy similarity
    Modified residuei168 – 1681N6-acetyllysineBy similarity
    Modified residuei225 – 2251N6-acetyllysine; alternateBy similarity
    Modified residuei225 – 2251N6-succinyllysine; alternateBy similarity
    Modified residuei232 – 2321N6-acetyllysineBy similarity
    Modified residuei241 – 2411N6-acetyllysineBy similarity
    Modified residuei244 – 2441N6-acetyllysineBy similarity
    Modified residuei249 – 2491N6-acetyllysineBy similarity
    Modified residuei251 – 2511N6-acetyllysine; alternateBy similarity
    Modified residuei251 – 2511N6-succinyllysine; alternateBy similarity
    Modified residuei353 – 3531N6-acetyllysine; alternateBy similarity
    Modified residuei353 – 3531N6-succinyllysine; alternateBy similarity
    Modified residuei369 – 3691N6-acetyllysineBy similarity
    Modified residuei382 – 3821N6-acetyllysineBy similarity
    Modified residuei411 – 4111N6-acetyllysineBy similarity

    Post-translational modificationi

    Acetylation at Lys-382 dramatically reduces catalytic activity. Deacetylated by SIRT3 By similarity.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP33198.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000002027.

    Structurei

    Secondary structure

    1
    421
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 235
    Helixi26 – 3813
    Turni39 – 435
    Beta strandi48 – 525
    Helixi55 – 606
    Turni61 – 633
    Helixi64 – 7613
    Beta strandi77 – 815
    Helixi89 – 957
    Helixi104 – 1129
    Beta strandi114 – 1207
    Beta strandi137 – 1426
    Helixi146 – 1494
    Beta strandi151 – 1555
    Beta strandi157 – 16711
    Beta strandi174 – 18310
    Beta strandi185 – 1939
    Helixi194 – 21118
    Beta strandi215 – 2195
    Turni221 – 2233
    Helixi227 – 24216
    Helixi244 – 2496
    Beta strandi254 – 2585
    Helixi259 – 26810
    Beta strandi273 – 2775
    Helixi279 – 29315
    Beta strandi298 – 3047
    Beta strandi311 – 3144
    Helixi321 – 3288
    Helixi338 – 35518
    Helixi358 – 37619
    Helixi382 – 3898
    Turni396 – 3983
    Helixi403 – 41917

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LWDX-ray1.85A/B9-421[»]
    ProteinModelPortaliP33198.
    SMRiP33198. Positions 9-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP33198.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni103 – 1097Substrate binding

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0538.
    HOGENOMiHOG000019858.
    HOVERGENiHBG006119.

    Family and domain databases

    Gene3Di3.40.718.10. 1 hit.
    InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
    IPR004790. Isocitrate_DH_NADP.
    IPR024084. IsoPropMal-DH-like_dom.
    [Graphical view]
    PANTHERiPTHR11822. PTHR11822. 1 hit.
    PfamiPF00180. Iso_dh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000108. IDH_NADP. 1 hit.
    TIGRFAMsiTIGR00127. nadp_idh_euk. 1 hit.
    PROSITEiPS00470. IDH_IMDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

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

    P33198-1 [UniParc]FASTAAdd to Basket

    « Hide

    ARAAARHYAD QRIKVAKPVV EMDGDEMTRI IWQFIKEKLI LPHVDVQLKY    50
    FDLGLPNRDQ TNDQVTIDSA LATQKYSVAV KCATITPDEA RVEEFKLKKM 100
    WKSPNGTIRN ILGGTVFREP IICKNIPRLV PGWTKPITIG RHAHGDQYKA 150
    TDFVVDRAGT FKIVFTPKDG SSAKQWEVYN FPAGGVGMGM YNTDESISGF 200
    AHSCFQYAIQ KKWPLYMSTK NTILKAYDGR FKDIFQEIFE KHYKTDFDKY 250
    KIWYEHRLID DMVAQVLKSS GGFVWACKNY DGDVQSDILA QGFGSLGLMT 300
    SVLVCPDGKT IEAEAAHGTV TRHYREHQKG RPTSTNPIAS IFAWTRGLEH 350
    RGKLDGNQDL IRFAQTLEKV CVETVESGAM TKDLAGCIHG LSNVKLNEHF 400
    LNTSDFLDTI KSNLDRALGR Q 421
    Length:421
    Mass (Da):47,526
    Last modified:February 1, 1994 - v1
    Checksum:i14862D47C00A053F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86719 mRNA. Translation: AAA31089.1.
    PIRiA43294.
    UniGeneiSsc.58398.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86719 mRNA. Translation: AAA31089.1 .
    PIRi A43294.
    UniGenei Ssc.58398.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LWD X-ray 1.85 A/B 9-421 [» ]
    ProteinModelPortali P33198.
    SMRi P33198. Positions 9-421.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9823.ENSSSCP00000002027.

    Proteomic databases

    PaxDbi P33198.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0538.
    HOGENOMi HOG000019858.
    HOVERGENi HBG006119.

    Enzyme and pathway databases

    Reactomei REACT_217226. Citric acid cycle (TCA cycle).
    SABIO-RK P33198.

    Miscellaneous databases

    EvolutionaryTracei P33198.

    Family and domain databases

    Gene3Di 3.40.718.10. 1 hit.
    InterProi IPR019818. IsoCit/isopropylmalate_DH_CS.
    IPR004790. Isocitrate_DH_NADP.
    IPR024084. IsoPropMal-DH-like_dom.
    [Graphical view ]
    PANTHERi PTHR11822. PTHR11822. 1 hit.
    Pfami PF00180. Iso_dh. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000108. IDH_NADP. 1 hit.
    TIGRFAMsi TIGR00127. nadp_idh_euk. 1 hit.
    PROSITEi PS00470. IDH_IMDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and sequence of a cDNA encoding porcine mitochondrial NADP-specific isocitrate dehydrogenase."
      Haselbeck R.J., Colman R.F., McAlister-Henn L.
      Biochemistry 31:6219-6223(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cysteinyl peptides of pig heart NADP-dependent isocitrate dehydrogenase that are modified upon inactivation by N-ethylmaleimide."
      Smyth G.E., Colman R.F.
      J. Biol. Chem. 266:14918-14925(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 82-91; 59-64; 201-211; 269-278 AND 369-392.
      Tissue: Heart.
    3. "Characterization of an active site peptide modified by the substrate analogue 3-bromo-2-ketoglutarate on a single chain of dimeric NADP+-dependent isocitrate dehydrogenase."
      Ehrlich R.S., Colman R.F.
      J. Biol. Chem. 262:12614-12619(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 383-395.
    4. "Critical role of Lys212 and Tyr140 in porcine NADP-dependent isocitrate dehydrogenase."
      Kim T.K., Lee P., Colman R.F.
      J. Biol. Chem. 278:49323-49331(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME KINETICS, MUTAGENESIS OF TRY-148 AND LYS-220.
    5. "Crystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanism."
      Ceccarelli C., Grodsky N.B., Ariyaratne N., Colman R.F., Bahnson B.J.
      J. Biol. Chem. 277:43454-43462(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 9-421 IN COMPLEX WITH MANGANESE AND ISOCITRATE, SUBUNIT.

    Entry informationi

    Entry nameiIDHP_PIG
    AccessioniPrimary (citable) accession number: P33198
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, 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

    External Data

    Dasty 3