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UniProtKB/Swiss-Prot entry Q9USP8


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

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Entry information
Entry name IDH2_SCHPO
Primary accession number Q9USP8
Secondary accession numbers None
Integrated into Swiss-Prot on February 21, 2001
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 60)
Name and origin of the protein
Protein name Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial [Precursor]
Synonyms EC 1.1.1.41
Isocitric dehydrogenase
NAD(+)-specific ICDH
Gene name
Name: idh2
ORFNames: SPBC902.05c
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
RNA-BINDING.
DOI=10.1007/s002940000132; PubMed=10975257 [NCBI, ExPASy, EBI, Israel, Japan]
Elzinga S.D.J., van Oosterum K., Maat C., Grivell L.A., van der Spek H.;
"Isolation and RNA-binding analysis of NAD+ -isocitrate dehydrogenases from Kluyveromyces lactis and Schizosaccharomyces pombe.";
Curr. Genet. 38:87-94(2000).
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
CU329671; CAB62099.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T50386; T50386.
RefSeq NP_595203.1; -.
3D structure databases
HSSP P39126; 1HQS. [HSSP ENTRY / PDB]
ModBase Q9USP8.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-003292-MON; -.
Organism-specific databases
GeneDB_Spombe SPBC902.05c; -.
Gene expression databases
ArrayExpress Q9USP8; -.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from InterPro).
GO:0004449; Molecular function: isocitrate dehydrogenase (NAD+) 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:0003723; Molecular function: RNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006537; Biological process: glutamate biosynthetic process (inferred from mutant phenotype from GeneDB_SPombe).
GO:0006102; Biological process: isocitrate metabolic process (inferred from mutant phenotype from GeneDB_SPombe).
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 InterPro).
QuickGo view.
Family and domain databases
InterPro IPR004434; IsoCit_DHase_NAD_mit.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.718.10; IDH_IMDH; 1.
PANTHER PTHR11835; IDH_IMDH_dimeric; 1.
Pfam PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00175; mito_nad_idh; 1.
PROSITE PS00470; IDH_IMDH; 1.
BLOCKS Q9USP8.
ProtoNet Q9USP8.
Genome annotation databases
GeneID 2541260; -.
KEGG spo:SPBC902.05c; -.
NMPDR fig|4896.1.peg.1069; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Magnesium; Manganese; Metal-binding; Mitochondrion; NAD; Oxidoreductase; RNA-binding; Transit peptide; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Mitochondrion (Potential). 
CHAIN   ?   378        Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial. PRO_0000014433
METAL   246   246        Magnesium or manganese (By similarity). 
METAL   272   272        Magnesium or manganese (By similarity). 
METAL   276   276        Magnesium or manganese (By similarity). 
BINDING   128   128        Substrate (By similarity). 
BINDING   138   138        Substrate (By similarity). 
BINDING   159   159        Substrate (By similarity). 
BINDING   246   246        Substrate (By similarity). 
SITE   166   166  1     Critical for catalysis (By similarity). 
SITE   213   213  1     Critical for catalysis (By similarity). 
Sequence information
Length: 378 AA [This is the length of the unprocessed precursor] Molecular weight: 41060 Da [This is the MW of the unprocessed precursor] CRC64: F2C03935DDC90FA2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSMLSTLRTA GSLRTFSRSA CYSFRFSSTK AAAGTYEGVK NANGNYTVTM IAGDGIGPEI 

        70         80         90        100        110        120 
AQSVERIFKA AKVPIEWERV KVYPILKNGT TTIPDDAKES VRKNKVALKG PLATPIGKGH 

       130        140        150        160        170        180 
VSMNLTLRRT FGLFANVRPC VSITGYKTPY DNVNTVLIRE NTEGEYSGIE HEVIPGVVQS 

       190        200        210        220        230        240 
IKLITRAASE RVIRYAFQYA RQTGKNNITV VHKATIMRMA DGLFLECAKE LAPEYPDIEL 

       250        260        270        280        290        300 
REEILDNACL KIVTDPVPYN NTVMVMPNLY GDIVSDMCAG LIGGLGLTPS GNIGNQASIF 

       310        320        330        340        350        360 
EAVHGTAPDI AGKGLANPTA LLLSSVMMLK HMNLNDYAKR IESAIFDTLA NNPDARTKDL 

       370 
GGKSNNVQYT DAIISKLK 

Q9USP8 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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