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Reviewed, UniProtKB/Swiss-Prot P33198 (IDHP_PIG)

Last modified June 16, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Isocitrate dehydrogenase [NADP], mitochondrial
      Short name=IDH
    EC=1.1.1.42
Alternative name(s):
    Oxalosuccinate decarboxylase
    NADP(+)-specific ICDH
    IDP
    ICD-M
Gene names
Name: IDH2
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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Protein attributes

Sequence length421 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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

Catalytic activity

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

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

Cofactor

Binds 1 magnesium or manganese ion per subunit.

Subunit structure

Homodimer. Ref.5

Subcellular location

Mitochondrion.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

biophysicochemical properties

Kinetic parameters:

KM=7.47 µM for isocitrate Ref.4

KM=9.85 µM for NADP

KM=0.11 µM for manganese

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

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide‹1 – 8›8Mitochondrion
Chain9 – 421413Isocitrate dehydrogenase [NADP], mitochondrial
PRO_0000014422

Regions

Nucleotide binding84 – 863NADP By similarity
Nucleotide binding318 – 3236NADP By similarity
Region103 – 1097Substrate binding

Sites

Metal binding2601Magnesium or manganese
Metal binding2831Magnesium or manganese
Binding site861Substrate
Binding site911NADP By similarity
Binding site1181Substrate
Binding site1411Substrate
Binding site2681NADP By similarity
Binding site3361NADP; via amide nitrogen and carbonyl oxygen
Site1481Critical for catalysis
Site2201Critical for catalysis

Amino acid modifications

Modified residue751N6-acetyllysine By similarity
Modified residue2411N6-acetyllysine By similarity

Experimental info

Mutagenesis1481Y → F: Large decrease in Vmax and insignificant change in KM for isocitrate and NADP. Ref.4
Mutagenesis2201K → Q or Y: Large decrease in Vmax and insignificant change in KM for isocitrate and NADP. Ref.4
Non-terminal residue11

Secondary structure

1 ............................................................... 421
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P33198-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 14862D47C00A053F

FASTA42147,526
        10         20         30         40         50         60 
ARAAARHYAD QRIKVAKPVV EMDGDEMTRI IWQFIKEKLI LPHVDVQLKY FDLGLPNRDQ 

        70         80         90        100        110        120 
TNDQVTIDSA LATQKYSVAV KCATITPDEA RVEEFKLKKM WKSPNGTIRN ILGGTVFREP 

       130        140        150        160        170        180 
IICKNIPRLV PGWTKPITIG RHAHGDQYKA TDFVVDRAGT FKIVFTPKDG SSAKQWEVYN 

       190        200        210        220        230        240 
FPAGGVGMGM YNTDESISGF AHSCFQYAIQ KKWPLYMSTK NTILKAYDGR FKDIFQEIFE 

       250        260        270        280        290        300 
KHYKTDFDKY KIWYEHRLID DMVAQVLKSS GGFVWACKNY DGDVQSDILA QGFGSLGLMT 

       310        320        330        340        350        360 
SVLVCPDGKT IEAEAAHGTV TRHYREHQKG RPTSTNPIAS IFAWTRGLEH RGKLDGNQDL 

       370        380        390        400        410        420 
IRFAQTLEKV CVETVESGAM TKDLAGCIHG LSNVKLNEHF LNTSDFLDTI KSNLDRALGR 


Q

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References

[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: 1627563] [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: 1869531] [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: 3624273] [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: 14512428] [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: 12207025] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 9-421 IN COMPLEX WITH MANGANESE AND ISOCITRATE, SUBUNIT.

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Cross-references

Sequence databases

M86719 mRNA. Translation: AAA31089.1.
PIRA43294.
UniGeneSsc.2449

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1LWDX-ray1.85A/B9-421[»]
ModBaseSearch...

Phylogenomic databases

HOVERGENP33198.

Enzyme and pathway databases

BRENDA1.1.1.42. 249.

Family and domain databases

InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR004790. Isocitrate_DH_NADP-dep_euk.
[Graphical view]
Gene3DG3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHERPTHR11822. IDH_NADP_euk. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000108. IDH_NADP. 1 hit.
TIGRFAMsTIGR00127. nadp_idh_euk. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameIDHP_PIG
AccessionPrimary (citable) accession number: P33198
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents