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Q5R9C5 (IDHC_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isocitrate dehydrogenase [NADP] cytoplasmic

Short name=IDH
EC=1.1.1.42
Alternative name(s):
Cytosolic NADP-isocitrate dehydrogenase
IDP
NADP(+)-specific ICDH
Oxalosuccinate decarboxylase
Gene names
Name:IDH1
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length414 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Post-translational modification

Acetylation at Lys-374 dramatically reduces catalytic activity By similarity.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 414413Isocitrate dehydrogenase [NADP] cytoplasmic
PRO_0000236187

Regions

Nucleotide binding75 – 773NADP By similarity
Nucleotide binding310 – 3156NADP By similarity
Region94 – 1007Substrate binding By similarity

Sites

Metal binding2521Magnesium or manganese By similarity
Metal binding2751Magnesium or manganese By similarity
Binding site771Substrate By similarity
Binding site821NADP By similarity
Binding site1091Substrate By similarity
Binding site1321Substrate By similarity
Binding site2601NADP By similarity
Binding site3281NADP; via amide nitrogen and carbonyl oxygen By similarity
Site1391Critical for catalysis By similarity
Site2121Critical for catalysis By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue811N6-acetyllysine By similarity
Modified residue1261N6-succinyllysine By similarity
Modified residue2241N6-acetyllysine By similarity
Modified residue2331N6-acetyllysine By similarity
Modified residue2431N6-acetyllysine By similarity
Modified residue3211N6-acetyllysine By similarity
Modified residue4001N6-succinyllysine By similarity

Experimental info

Sequence conflict251L → Q in CAH89719. Ref.1
Sequence conflict2261I → T in CAH91635. Ref.1
Sequence conflict3311A → V in CAH91635. Ref.1
Sequence conflict4111Q → L in CAH89719. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5R9C5 [UniParc].

Last modified May 30, 2006. Version 2.
Checksum: 73CB3A9AC5E411BA

FASTA41446,699
        10         20         30         40         50         60 
MSKKISGGSV VEMQGDEMTR IIWELIKEKL IFPYVELDLH SYDLGIENRD ATNDQVTKDA 

        70         80         90        100        110        120 
AEAIKKYNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR NILGGTVFRE AIICKNIPRL 

       130        140        150        160        170        180 
VSGWVKPIII GRHAYGDQYR ATDFVVPGPG KVEITYTPSD GTQKVTYLVH NFEEGGGVAM 

       190        200        210        220        230        240 
GMYNQDKSIE DFAHSSFQMA LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKQYKSQFE 

       250        260        270        280        290        300 
ARKIWYEHRL IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLVCPDG 

       310        320        330        340        350        360 
KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWTRGL AHRAKLDNNK ELAFFANALE 

       370        380        390        400        410 
EVSVETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK LGENLKIKLA QAKL 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR857428 mRNA. Translation: CAH89719.1.
CR859464 mRNA. Translation: CAH91635.1.
RefSeqNP_001124781.1. NM_001131309.1.

3D structure databases

ProteinModelPortalQ5R9C5.
SMRQ5R9C5. Positions 1-414.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5R9C5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSPPYT00000015262; ENSPPYP00000014668; ENSPPYG00000013125.
GeneID100171634.
KEGGpon:100171634.

Organism-specific databases

CTD3417.

Phylogenomic databases

GeneTreeENSGT00390000012547.
HOVERGENHBG006119.
InParanoidQ5R9C5.
KOK00031.
OMASCGGVAM.
OrthoDBEOG7QNVKS.
TreeFamTF300428.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR004790. Isocitrate_DH_NADP.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERPTHR11822. PTHR11822. 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...

Entry information

Entry nameIDHC_PONAB
AccessionPrimary (citable) accession number: Q5R9C5
Secondary accession number(s): Q5RET8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: May 30, 2006
Last modified: May 14, 2014
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families