Isocitrate dehydrogenase [NADP], mitochondrial precursor

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Reviewed, UniProtKB/Swiss-Prot Q04467 (IDHP_BOVIN)

Last modified November 3, 2009. Version 69. History...

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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 names

Recommended 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

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 By similarity.
Subunit structure	Homodimer.
Subcellular location	Mitochondrion.
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family.

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Ontologies

Keywords
Biological process	Glyoxylate bypass Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Magnesium Manganese Metal-binding NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	glyoxylate cycle Inferred from electronic annotation. Source: UniProtKB-KW isocitrate metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial inner membrane Inferred from sequence or structural similarity. Source: AgBase
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro isocitrate dehydrogenase (NADP+) activity Inferred from sequence or structural similarity. Source: AgBase magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 39

Mitochondrion Ref.1

Chain

40 – 452

413

Isocitrate dehydrogenase [NADP], mitochondrial

PRO_0000014419

Regions

Nucleotide binding

115 – 117

NADP By similarity

Nucleotide binding

349 – 354

NADP By similarity

Region

134 – 140

Substrate binding By similarity

Sites

Metal binding

291

Magnesium or manganese By similarity

Metal binding

314

Magnesium or manganese By similarity

Binding site

117

Substrate By similarity

Binding site

122

NADP By similarity

Binding site

149

Substrate By similarity

Binding site

172

Substrate By similarity

Binding site

299

NADP By similarity

Binding site

367

NADP; via amide nitrogen and carbonyl oxygen By similarity

Site

179

Critical for catalysis By similarity

Site

251

Critical for catalysis By similarity

Amino acid modifications

Modified residue

N6-acetyllysine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

106

N6-acetyllysine By similarity

Modified residue

133

N6-acetyllysine By similarity

Modified residue

155

N6-acetyllysine By similarity

Modified residue

166

N6-acetyllysine By similarity

Modified residue

180

N6-acetyllysine By similarity

Modified residue

256

N6-acetyllysine By similarity

Modified residue

263

N6-acetyllysine By similarity

Modified residue

272

N6-acetyllysine By similarity

Modified residue

275

N6-acetyllysine By similarity

Modified residue

282

N6-acetyllysine By similarity

Modified residue

442

N6-acetyllysine By similarity

Experimental info

Sequence conflict

A → R in CAA49207. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q04467-1 [UniParc].

Last modified May 30, 2006. Version 2.
Checksum: FAB87D3C624E0C71
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FASTA

452

50,739

        10         20         30         40         50         60 
MAGYLRVVRS LCRASGSGSA WAPAALTAPN LQEQPRRHYA DKRIKVAKPV VEMDGDEMTR 

        70         80         90        100        110        120 
IIWQFIKEKL ILPHVDVQLK YFDLGLPNRD QTNDQVTIDS ALATQKYSVA VKCATITPDE 

       130        140        150        160        170        180 
ARVEEFKLKK MWKSPNGTIR NILGGTVFRE PIICKNIPRL VPGWTKPITI GRHAHGDQYK 

       190        200        210        220        230        240 
ATDFVVDRAG TFKVVFTPKD GSGPKEWEVY NFPAGGVGMG MYNTDESISG FAHSCFQYAI 

       250        260        270        280        290        300 
QKKWPLYMST KNTILKAYDG RFKDIFQAIF EKHYKTEFDK HKIWYEHRLI DDMVAQVLKS 

       310        320        330        340        350        360 
SGGFVWACKN YDGDVQSDIL AQGFGSLGLM TSVLVCPDGK TIEAEAAHGT VTRHYREHQK 

       370        380        390        400        410        420 
GRPTSTNPIA SIFAWTRGLE HRGKLDGNQD LIRFAQTLEK VCVETVESGA MTKDLAGCIH 

       430        440        450 
GLSNVKLNEH FLNTSDFLDT IKSNLDRALG QQ

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a cDNA encoding bovine mitochondrial NADP(+)-specific isocitrate dehydrogenase and structural comparison with its isoenzymes from different species." Huh T.-L., Ryu J.-H., Huh J.-W., Sung H.-C., Oh I.-U., Song B.J., Veech R.L. Biochem. J. 292:705-710(1993) [PubMed: 8318002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 40-55. Tissue: Kidney.
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Ileum.

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Cross-references

Sequence databases
	X69432 mRNA. Translation: CAA49207.1. BC102509 mRNA. Translation: AAI02510.1.
IPI	IPI00714468.
PIR	S33859.
RefSeq	NP_786984.1.
UniGene	Bt.5520
3D structure databases
HSSP	HSSP built from PDB template 1LWD based on UniProtKB P33198.
SMR	Q04467. Positions 40-452.
ModBase	Search...
Protein-protein interaction databases
STRING	Q04467.
Genome annotation databases
Ensembl	ENSBTAT00000018741; ENSBTAP00000018741; ENSBTAG00000014093; Bos taurus. [Genome view]
GeneID	327669.
KEGG	bta:327669.
Organism-specific databases
CTD	327669.
Phylogenomic databases
HOVERGEN	Q04467.
OMA	GGMLWAC.
Enzyme and pathway databases
BRENDA	1.1.1.42. 251.
Family and domain databases
InterPro	IPR019818. IsoCit/isopropylmalate_DH_CS. IPR001804. Isocitrate/isopropylmalate_DH. IPR004790. Isocitrate_DH_NADP-dep_euk. [Graphical view]
Gene3D	G3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHER	PTHR11822. IDH_NADP_euk. 1 hit.
Pfam	PF00180. Iso_dh. 1 hit. [Graphical view]
PIRSF	PIRSF000108. IDH_NADP. 1 hit.
TIGRFAMs	TIGR00127. nadp_idh_euk. 1 hit.
PROSITE	PS00470. IDH_IMDH. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

IDHP_BOVIN

Accession

Primary (citable) accession number: Q04467
Secondary accession number(s): Q3ZCD4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	May 30, 2006
Last modified:	November 3, 2009
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents