[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 40-55. TISSUE=Kidney; PubMed=8318002 [NCBI, ExPASy, EBI, Israel, Japan] Huh T.-L., Ryu J.-H., Huh J.-W., Sung H.-C., Oh I.-U., Song B.J., Veech R.L.; "Cloning of a cDNA encoding bovine mitochondrial NADP(+)-specific isocitrate dehydrogenase and structural comparison with its isoenzymes from different species."; Biochem. J. 292:705-710(1993).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Crossbred X Angus; TISSUE=Ileum; NIH - Mammalian Gene Collection (MGC) project; Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.

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.
CATALYTIC ACTIVITY: Oxalosuccinate + NADP⁺ = 2-oxoglutarate + CO₂ + NADPH.
COFACTOR: Binds 1 magnesium or manganese ion per subunit (By similarity).
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Mitochondrion.
SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X69432; CAA49207.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC102509; AAI02510.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S33859; S33859.

NP_786984.1; -.

3D structure databases

HSSP

P33198; 1LWD. [HSSP ENTRY / PDB]

SMR

Q04467; 40-452.

ModBase

Q04467.

Ontologies

GO:0005743;	Cellular component: mitochondrial inner membrane (inferred from sequence or structural similarity from AgBase).
GO:0004450;	Molecular function: isocitrate dehydrogenase (NADP+) activity (inferred from sequence or structural similarity from AgBase).
QuickGo view.

Family and domain databases

InterPro

IPR004790; IsoCit_DHase_NADP-dep_euk.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.718.10; IDH_IMDH; 1.

PANTHER

PTHR11822; IDH_NADP_euk; 1.

Pfam

PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000108; IDH_NADP; 1.

TIGRFAMs

TIGR00127; nadp_idh_euk; 1.

PROSITE

PS00470; IDH_IMDH; 1.

Genome annotation databases

Ensembl

ENSBTAG00000014093; Bos taurus. [Contig view]

GeneID

327669; -.

KEGG

bta:327669; -.

Phylogenomic databases

HOVERGEN

Q04467; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Direct protein sequencing; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; Mitochondrion; NADP; Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 39`	`39`	`Mitochondrion.`
`CHAIN`	`40 452`	`413`	`Isocitrate dehydrogenase [NADP], mitochondrial.`	`PRO_0000014419`
`NP_BIND`	`115 117`	`3`	`NADP (By similarity).`
`NP_BIND`	`349 354`	`6`	`NADP (By similarity).`
`REGION`	`134 140`	`7`	`Substrate binding (By similarity).`
`METAL`	`291 291`		`Magnesium or manganese (By similarity).`
`METAL`	`314 314`		`Magnesium or manganese (By similarity).`
`BINDING`	`117 117`		`Substrate (By similarity).`
`BINDING`	`122 122`		`NADP (By similarity).`
`BINDING`	`149 149`		`Substrate (By similarity).`
`BINDING`	`172 172`		`Substrate (By similarity).`
`BINDING`	`299 299`		`NADP (By similarity).`
`BINDING`	`367 367`		`NADP; via amide nitrogen and carbonyl oxygen (By similarity).`
`SITE`	`179 179`	`1`	`Critical for catalysis (By similarity).`
`SITE`	`251 251`	`1`	`Critical for catalysis (By similarity).`
`MOD_RES`	`106 106`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`272 272`		`N6-acetyllysine (By similarity).`
`CONFLICT`	`24 24`		`A -> R (in Ref. 1; CAA49207).`

Sequence information

Length: 452 AA [This is the length of the unprocessed precursor]

Molecular weight: 50739 Da [This is the MW of the unprocessed precursor]

CRC64: FAB87D3C624E0C71 [This is a checksum on the sequence]

        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

Q04467 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools