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UniProtKB/Swiss-Prot entry Q75JR2

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IDHP_DICDI
Primary accession number Q75JR2
Secondary accession number Q559Q0
Integrated into Swiss-Prot on April 8, 2008
Sequence was last modified on July 5, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 32)
Name and origin of the protein
Protein name Isocitrate dehydrogenase [NADP], mitochondrial [Precursor]
Synonyms EC 1.1.1.42
IDH 2
NADP-isocitrate dehydrogenase 2
Oxalosuccinate decarboxylase 2
NADP(+)-specific ICDH 2
IDP 2
Gene name
Name: idhM
ORFNames: DDB_G0272210
From
Dictyostelium discoideum (Slime mold) [TaxID: 44689] 
Taxonomy Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
DOI=10.1038/nature00847; PubMed=12097910 [NCBI, ExPASy, EBI, Israel, Japan]
Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A., Noegel A.A.;
"Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
Nature 418:79-85(2002).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
DOI=10.1038/nature03481; PubMed=15875012 [NCBI, ExPASy, EBI, Israel, Japan]
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
Comments
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
AC116963; AAS45362.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AAFI02000008; EAL71257.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_645284.1; -.
3D structure databases
ModBase Q75JR2.
Organism-specific databases
dictyBase DDB_G0272210; idhM.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0004450; Molecular function: isocitrate dehydrogenase (NADP+) activity (inferred from electronic annotation from InterPro).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145; Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006097; Biological process: glyoxylate cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0006102; Biological process: isocitrate metabolic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006099; Biological process: tricarboxylic acid cycle (inferred from electronic annotation from UniProtKB-KW).
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.
ProtoNet Q75JR2.
Genome annotation databases
GeneID 3396433; -.
KEGG ddi:DDB_0231402; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; Mitochondrion; NADP; Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    27  27     Mitochondrion (Potential). 
CHAIN   28   428  401     Isocitrate dehydrogenase [NADP], mitochondrial. PRO_0000328191
NP_BIND   98   100  3     NADP (By similarity). 
NP_BIND   330   335  6     NADP (By similarity). 
REGION   117   123  7     Substrate binding (By similarity). 
METAL   273   273        Magnesium or manganese (By similarity). 
METAL   296   296        Magnesium or manganese (By similarity). 
BINDING   100   100        Substrate (By similarity). 
BINDING   105   105        NADP (By similarity). 
BINDING   132   132        Substrate (By similarity). 
BINDING   155   155        Substrate (By similarity). 
BINDING   281   281        NADP (By similarity). 
BINDING   348   348        NADP; via amide nitrogen and carbonyl oxygen (By similarity). 
SITE   162   162  1     Critical for catalysis (By similarity). 
SITE   233   233  1     Critical for catalysis (By similarity). 
Sequence information
Length: 428 AA [This is the length of the unprocessed precursor] Molecular weight: 48064 Da [This is the MW of the unprocessed precursor] CRC64: C91B168940882AE1 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MISNISKKIL SNSSKFIQQQ SYSTKRIKVT GPVVEMDGDE QTRIMWESIK SKLIFPYVDI 

        70         80         90        100        110        120 
TPEYYDLGLP NRDATNDQVT IDAANAIKRA KIGVKCATIT PDEARVKEFG LKEMWKSPNG 

       130        140        150        160        170        180 
TIRNILDGTV FRGPIICKNL PLLVPGWKKP IIIGRHAHGD QYKATDFVVN GPGKLEMIFT 

       190        200        210        220        230        240 
PSQGEPIKKV IYDFKGSGVA MGMYNTTSSI TAFAHSCFQY AIDKKYPLYL STKNTILKKY 

       250        260        270        280        290        300 
DGQFKDIFQE IYEREYSTKF GELGIWYEHR LIDDMVAFAL KSEGGFVWAC KNYDGDVQSD 

       310        320        330        340        350        360 
IVAQGYGSLG LMTSVLTNAD GVFASEASHG TVTRHFREHQ KGNETSTNSV ASIFAWTSAL 

       370        380        390        400        410        420 
GQRGKLDNNK DLVKFAQDME KACVESIESG FMTKDLAICI KGNQVKRSNY LNTEEYINKV 


AEFYNKIK
Q75JR2 in FASTA format

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