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UniProtKB/Swiss-Prot entry O13696

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

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Entry information
Entry name IDH1_SCHPO
Primary accession number O13696
Secondary accession numbers None
Integrated into Swiss-Prot on February 21, 2001
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 67)
Name and origin of the protein
Protein name Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial [Precursor]
Synonyms EC 1.1.1.41
Isocitric dehydrogenase
NAD(+)-specific ICDH
Gene name
Name: idh1
ORFNames: SPAC11G7.03
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
CU329670; CAB16208.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T37546; T37546.
RefSeq NP_594397.1; -.
3D structure databases
HSSP P08200; 1ISO. [HSSP ENTRY / PDB]
ModBase O13696.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-002502-MON; -.
Organism-specific databases
GeneDB_Spombe SPAC11G7.03; -.
Gene expression databases
ArrayExpress O13696; -.
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.
Genome annotation databases
GeneID 2541894; -.
KEGG spo:SPAC11G7.03; -.
NMPDR fig|4896.1.peg.4367; -.
Other
ProtoNet O13696.
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   ?   356        Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial. PRO_0000014430
METAL   224   224        Magnesium or manganese (By similarity). 
BINDING   106   106        Substrate (By similarity). 
BINDING   137   137        Substrate (By similarity). 
BINDING   224   224        Substrate (By similarity). 
SITE   144   144  1     Critical for catalysis (By similarity). 
SITE   191   191  1     Critical for catalysis (By similarity). 
Sequence information
Length: 356 AA [This is the length of the unprocessed precursor] Molecular weight: 38758 Da [This is the MW of the unprocessed precursor] CRC64: 11B482F42B467AAC [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MFKSLVRKSS AFQPLKYGGK YTVTLIPGDG IGRETSNAVT EIFKTANVPI EFEEIDVTGM 

        70         80         90        100        110        120 
EKNNKSSGDA LHEAIQSLKR NKVGLKGILF TPFEKGGHTS FNVALRKELD IYASLVLIKN 

       130        140        150        160        170        180 
IPGFKTRHDN VDFAIIRENT EGEYSGLEHQ SVPGVVESLK IITEYKSKRI AQFAFDFALQ 

       190        200        210        220        230        240 
NGRKSVTCIH KANIMKLADG LFRRTFYDVA NGYDAITPKD LIVDNASMQA VSRPQQFDVL 

       250        260        270        280        290        300 
VMPNLYGSIL SNIGSALVGG PGVIPGANFG RDYALFEPGC RHVGLSITGR GEANPTAAIL 

       310        320        330        340        350 
SACLMLRHLG LKDYADLINA ATYSVIEEGK TLTKDLGGSA STGDFTHAIL ERMESL
O13696 in FASTA format

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