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P33198

- IDHP_PIG

UniProt

P33198 - IDHP_PIG

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Protein

Isocitrate dehydrogenase [NADP], mitochondrial

Gene

IDH2

Organism
Sus scrofa (Pig)
Status
Reviewed - 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 Mg(2+) or Mn(2+) 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
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

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
Complete GO annotation...

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 – 235Combined sources
Helixi26 – 3813Combined sources
Turni39 – 435Combined sources
Beta strandi48 – 525Combined sources
Helixi55 – 606Combined sources
Turni61 – 633Combined sources
Helixi64 – 7613Combined sources
Beta strandi77 – 815Combined sources
Helixi89 – 957Combined sources
Helixi104 – 1129Combined sources
Beta strandi114 – 1207Combined sources
Beta strandi137 – 1426Combined sources
Helixi146 – 1494Combined sources
Beta strandi151 – 1555Combined sources
Beta strandi157 – 16711Combined sources
Beta strandi174 – 18310Combined sources
Beta strandi185 – 1939Combined sources
Helixi194 – 21118Combined sources
Beta strandi215 – 2195Combined sources
Turni221 – 2233Combined sources
Helixi227 – 24216Combined sources
Helixi244 – 2496Combined sources
Beta strandi254 – 2585Combined sources
Helixi259 – 26810Combined sources
Beta strandi273 – 2775Combined sources
Helixi279 – 29315Combined sources
Beta strandi298 – 3047Combined sources
Beta strandi311 – 3144Combined sources
Helixi321 – 3288Combined sources
Helixi338 – 35518Combined sources
Helixi358 – 37619Combined sources
Helixi382 – 3898Combined sources
Turni396 – 3983Combined sources
Helixi403 – 41917Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP33198.

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

        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)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

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 .
PIRi A43294.
UniGenei Ssc.58398.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P33198.

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: November 26, 2014
This is version 101 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