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Protein

Isocitrate dehydrogenase [NADP], mitochondrial

Gene

IDH2

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Mg2+, Mn2+Note: Binds 1 Mg2+ or Mn2+ 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
  1. Vmax=39.6 µmol/min/mg enzyme with isocitrate as substrate

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei86Substrate1
Binding sitei91NADPBy similarity1
Binding sitei118Substrate1
Binding sitei141Substrate1
Sitei148Critical for catalysis1
Sitei220Critical for catalysis1
Metal bindingi260Magnesium or manganese1
Binding sitei268NADPBy similarity1
Metal bindingi283Magnesium or manganese1
Binding sitei336NADP; via amide nitrogen and carbonyl oxygen1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi84 – 86NADPBy similarity3
Nucleotide bindingi318 – 323NADPBy similarity6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glyoxylate bypass, Tricarboxylic acid cycle

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, NADP

Enzyme and pathway databases

BRENDAi1.1.1.42. 6170.
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
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi148Y → F: Large decrease in Vmax and insignificant change in KM for isocitrate and NADP. 1 Publication1
Mutagenesisi220K → Q or Y: Large decrease in Vmax and insignificant change in KM for isocitrate and NADP. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei‹1 – 8Mitochondrion›8
ChainiPRO_00000144229 – 421Isocitrate dehydrogenase [NADP], mitochondrialAdd BLAST413

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14N6-acetyllysineBy similarity1
Modified residuei17N6-acetyllysineBy similarity1
Modified residuei36N6-acetyllysineBy similarity1
Modified residuei38N6-acetyllysineBy similarity1
Modified residuei49N6-acetyllysine; alternateBy similarity1
Modified residuei49N6-succinyllysine; alternateBy similarity1
Modified residuei75N6-acetyllysine; alternateBy similarity1
Modified residuei75N6-succinyllysine; alternateBy similarity1
Modified residuei124N6-acetyllysineBy similarity1
Modified residuei135N6-acetyllysine; alternateBy similarity1
Modified residuei135N6-succinyllysine; alternateBy similarity1
Modified residuei149N6-acetyllysine; alternateBy similarity1
Modified residuei149N6-succinyllysine; alternateBy similarity1
Modified residuei162N6-acetyllysine; alternateBy similarity1
Modified residuei162N6-succinyllysine; alternateBy similarity1
Modified residuei168N6-acetyllysineBy similarity1
Modified residuei225N6-acetyllysine; alternateBy similarity1
Modified residuei225N6-succinyllysine; alternateBy similarity1
Modified residuei232N6-acetyllysineBy similarity1
Modified residuei241N6-acetyllysineBy similarity1
Modified residuei244N6-acetyllysineBy similarity1
Modified residuei249N6-acetyllysineBy similarity1
Modified residuei251N6-acetyllysine; alternateBy similarity1
Modified residuei251N6-succinyllysine; alternateBy similarity1
Modified residuei353N6-acetyllysine; alternateBy similarity1
Modified residuei353N6-succinyllysine; alternateBy similarity1
Modified residuei369N6-acetyllysineBy similarity1
Modified residuei382N6-acetyllysineBy similarity1
Modified residuei411N6-acetyllysineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP33198.
PeptideAtlasiP33198.
PRIDEiP33198.

Expressioni

Gene expression databases

BgeeiENSSSCG00000001852.
GenevisibleiP33198. SS.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000002026.

Structurei

Secondary structure

1421
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi19 – 23Combined sources5
Helixi26 – 38Combined sources13
Turni39 – 43Combined sources5
Beta strandi48 – 52Combined sources5
Helixi55 – 60Combined sources6
Turni61 – 63Combined sources3
Helixi64 – 76Combined sources13
Beta strandi77 – 81Combined sources5
Helixi89 – 95Combined sources7
Helixi104 – 112Combined sources9
Beta strandi114 – 120Combined sources7
Beta strandi137 – 142Combined sources6
Helixi146 – 149Combined sources4
Beta strandi151 – 155Combined sources5
Beta strandi157 – 167Combined sources11
Beta strandi174 – 183Combined sources10
Beta strandi185 – 193Combined sources9
Helixi194 – 211Combined sources18
Beta strandi215 – 219Combined sources5
Turni221 – 223Combined sources3
Helixi227 – 242Combined sources16
Helixi244 – 249Combined sources6
Beta strandi254 – 258Combined sources5
Helixi259 – 268Combined sources10
Beta strandi273 – 277Combined sources5
Helixi279 – 293Combined sources15
Beta strandi298 – 304Combined sources7
Beta strandi311 – 314Combined sources4
Helixi321 – 328Combined sources8
Helixi338 – 355Combined sources18
Helixi358 – 376Combined sources19
Helixi382 – 389Combined sources8
Turni396 – 398Combined sources3
Helixi403 – 419Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LWDX-ray1.85A/B9-421[»]
ProteinModelPortaliP33198.
SMRiP33198.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33198.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni103 – 109Substrate binding7

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1526. Eukaryota.
COG0538. LUCA.
HOGENOMiHOG000019858.
HOVERGENiHBG006119.
InParanoidiP33198.
OrthoDBiEOG091G06IY.

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.
SMARTiSM01329. Iso_dh. 1 hit.
[Graphical view]
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

        10         20         30         40         50
ARAAARHYAD QRIKVAKPVV EMDGDEMTRI IWQFIKEKLI LPHVDVQLKY
60 70 80 90 100
FDLGLPNRDQ TNDQVTIDSA LATQKYSVAV KCATITPDEA RVEEFKLKKM
110 120 130 140 150
WKSPNGTIRN ILGGTVFREP IICKNIPRLV PGWTKPITIG RHAHGDQYKA
160 170 180 190 200
TDFVVDRAGT FKIVFTPKDG SSAKQWEVYN FPAGGVGMGM YNTDESISGF
210 220 230 240 250
AHSCFQYAIQ KKWPLYMSTK NTILKAYDGR FKDIFQEIFE KHYKTDFDKY
260 270 280 290 300
KIWYEHRLID DMVAQVLKSS GGFVWACKNY DGDVQSDILA QGFGSLGLMT
310 320 330 340 350
SVLVCPDGKT IEAEAAHGTV TRHYREHQKG RPTSTNPIAS IFAWTRGLEH
360 370 380 390 400
RGKLDGNQDL IRFAQTLEKV CVETVESGAM TKDLAGCIHG LSNVKLNEHF
410 420
LNTSDFLDTI KSNLDRALGR Q
Length:421
Mass (Da):47,526
Last modified:February 1, 1994 - v1
Checksum:i14862D47C00A053F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86719 mRNA. Translation: AAA31089.1.
PIRiA43294.
UniGeneiSsc.58398.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86719 mRNA. Translation: AAA31089.1.
PIRiA43294.
UniGeneiSsc.58398.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LWDX-ray1.85A/B9-421[»]
ProteinModelPortaliP33198.
SMRiP33198.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000002026.

Proteomic databases

PaxDbiP33198.
PeptideAtlasiP33198.
PRIDEiP33198.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1526. Eukaryota.
COG0538. LUCA.
HOGENOMiHOG000019858.
HOVERGENiHBG006119.
InParanoidiP33198.
OrthoDBiEOG091G06IY.

Enzyme and pathway databases

BRENDAi1.1.1.42. 6170.
SABIO-RKP33198.

Miscellaneous databases

EvolutionaryTraceiP33198.

Gene expression databases

BgeeiENSSSCG00000001852.
GenevisibleiP33198. SS.

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.
SMARTiSM01329. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00127. nadp_idh_euk. 1 hit.
PROSITEiPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 117 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

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 one 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.