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Protein

Isocitrate dehydrogenase [NADP]

Gene

IDH1

Organism
Macaca mulatta (Rhesus macaque)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation, Mn2+UniRule annotationNote: Binds 1 Mg(2+) or Mn2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei77 – 771SubstrateUniRule annotation
Binding sitei82 – 821NADPUniRule annotation
Binding sitei109 – 1091SubstrateUniRule annotation
Binding sitei132 – 1321SubstrateUniRule annotation
Sitei139 – 1391Critical for catalysisUniRule annotation
Sitei212 – 2121Critical for catalysisUniRule annotation
Metal bindingi252 – 2521Magnesium or manganeseUniRule annotation
Binding sitei260 – 2601NADPUniRule annotation
Metal bindingi275 – 2751Magnesium or manganeseUniRule annotation
Binding sitei328 – 3281NADP; via amide nitrogen and carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi75 – 773NADPUniRule annotation
Nucleotide bindingi310 – 3156NADPUniRule annotation

GO - Molecular functioni

  1. isocitrate dehydrogenase (NADP+) activity Source: UniProtKB-EC
  2. magnesium ion binding Source: Ensembl
  3. NAD binding Source: InterPro

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: Ensembl
  2. glutathione metabolic process Source: Ensembl
  3. isocitrate metabolic process Source: InterPro
  4. response to oxidative stress Source: Ensembl
  5. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Biological processi

Tricarboxylic acid cycleUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, ManganeseUniRule annotation, Metal-bindingUniRule annotation, NADPUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate dehydrogenase [NADP]UniRule annotation (EC:1.1.1.42UniRule annotation)
Gene namesi
Name:IDH1Imported
OrganismiMacaca mulatta (Rhesus macaque)Imported
Taxonomic identifieri9544 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca
ProteomesiUP000006718: Chromosome 12

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. mitochondrion Source: Ensembl
  4. peroxisome Source: Ensembl
Complete GO annotation...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni94 – 1007Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the isocitrate and isopropylmalate dehydrogenases family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000012547.
KOiK00031.
OMAiHNFESCG.
OrthoDBiEOG7QNVKS.
TreeFamiTF300428.

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: Complete.

F7GN57-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKKISGGSV VELQGDEMTR IIWELIKEKL IFPYVELDLQ SYDLGIENRD
60 70 80 90 100
ATNDQVTKDA AEAIKKYNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR
110 120 130 140 150
NILGGTVFRE AIICKNIPRL VSGWVKPIII GRHAYGDQYR ATDFVVPGPG
160 170 180 190 200
KVEITYTPSD GTQKVTYLVH NFEEGGGVAM GMYNQDKSIE DFAHSSFQMA
210 220 230 240 250
LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKQYKSQFE AQKIWYEHRL
260 270 280 290 300
IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLVCPDG
310 320 330 340 350
KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWTRGL AHRAKLDNNK
360 370 380 390 400
ELAFFANALE EVCIETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK
410
LGENLKIKLA QAKL
Length:414
Mass (Da):46,674
Last modified:July 27, 2011 - v1
Checksum:i2C102DC5CF93452B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JV565009 mRNA. Translation: AFJ70344.1.
RefSeqiNP_001252708.1. NM_001265779.2.
UniGeneiMmu.2453.

Genome annotation databases

EnsembliENSMMUT00000022610; ENSMMUP00000021152; ENSMMUG00000016077.
ENSMMUT00000044755; ENSMMUP00000037774; ENSMMUG00000016077.
ENSMMUT00000044757; ENSMMUP00000037776; ENSMMUG00000016077.
GeneIDi710019.
KEGGimcc:710019.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JV565009 mRNA. Translation: AFJ70344.1.
RefSeqiNP_001252708.1. NM_001265779.2.
UniGeneiMmu.2453.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMMUT00000022610; ENSMMUP00000021152; ENSMMUG00000016077.
ENSMMUT00000044755; ENSMMUP00000037774; ENSMMUG00000016077.
ENSMMUT00000044757; ENSMMUP00000037776; ENSMMUG00000016077.
GeneIDi710019.
KEGGimcc:710019.

Organism-specific databases

CTDi3417.

Phylogenomic databases

GeneTreeiENSGT00390000012547.
KOiK00031.
OMAiHNFESCG.
OrthoDBiEOG7QNVKS.
TreeFamiTF300428.

Miscellaneous databases

NextBioi19961335.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Evolutionary and biomedical insights from the rhesus macaque genome."
    Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C., Makova K.D., Miller W., Milosavljevic A.
    , Palermo R.E., Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., Zwieg A.S.
    Science 316:222-234(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 17573Imported.
  2. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: 17573Imported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: BrainImported.

Entry informationi

Entry nameiF7GN57_MACMU
AccessioniPrimary (citable) accession number: F7GN57
Entry historyi
Integrated into UniProtKB/TrEMBL: July 27, 2011
Last sequence update: July 27, 2011
Last modified: February 4, 2015
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.