ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry O14254


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name IDHP_SCHPO
Primary accession number O14254
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 62)
Name and origin of the protein
Protein name Probable isocitrate dehydrogenase [NADP], mitochondrial [Precursor]
Synonyms IDH
EC 1.1.1.42
Oxalosuccinate decarboxylase
NADP(+)-specific ICDH
IDP
Gene name
Name: idp1
ORFNames: SPAC6G10.08
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 2: Evidence at transcript 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).
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; CAB11294.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T39058; T39058.
RefSeq NP_594105.1; -.
3D structure databases
HSSP P33198; 1LWD. [HSSP ENTRY / PDB]
ModBase O14254.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-001728-MON; -.
Organism-specific databases
GeneDB_Spombe SPAC6G10.08; -.
Gene expression databases
ArrayExpress O14254; -.
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: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.
Genome annotation databases
GeneID 2542598; -.
KEGG spo:SPAC6G10.08; -.
NMPDR fig|4896.1.peg.4075; -.
Other
ProtoNet O14254.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Magnesium; Manganese; Metal-binding; Mitochondrion; NADP; Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Mitochondrion. 
CHAIN   ?   418        Probable isocitrate dehydrogenase [NADP], mitochondrial. PRO_0000014425
NP_BIND   85    87  3     NADP (By similarity). 
NP_BIND   320   325  6     NADP (By similarity). 
REGION   104   110  7     Substrate binding (By similarity). 
METAL   262   262        Magnesium or manganese (By similarity). 
METAL   285   285        Magnesium or manganese (By similarity). 
BINDING   87    87        Substrate (By similarity). 
BINDING   92    92        NADP (By similarity). 
BINDING   119   119        Substrate (By similarity). 
BINDING   142   142        Substrate (By similarity). 
BINDING   270   270        NADP (By similarity). 
BINDING   338   338        NADP; via amide nitrogen and carbonyl oxygen (By similarity). 
SITE   149   149  1     Critical for catalysis (By similarity). 
SITE   222   222  1     Critical for catalysis (By similarity). 
Sequence information
Length: 418 AA [This is the length of the unprocessed precursor] Molecular weight: 47293 Da [This is the MW of the unprocessed precursor] CRC64: 6E114B379C8AD61E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNMRMASSKS FQKITVKNPV VEMDGDEMTR VIWKIIREKL VLPYMDIKLD YYDLGIEARD 

        70         80         90        100        110        120 
KTNDQITVDA AKAILKNDVG IKCATITPDE ARVKEYNLKK MWKSPNGTIR NILNGTVFRE 

       130        140        150        160        170        180 
PILIKNIPKY IPGWTNPICI GRHAFGDQYK STDLVASGPG KLELSFTPKG NPSAKETYNV 

       190        200        210        220        230        240 
YEFNGSGVAM SMYNTDDSIR GFAHSSFQMA LQKKMPLYLS TKNTILKKYD GRFKDTFQEV 

       250        260        270        280        290        300 
YESDYKQKFE ELGLWYQHRL IDDMVAQAIK SNGGFVWACK NYDGDVMSDV VAQAYGSLGL 

       310        320        330        340        350        360 
MTSVLIHPNG RTFESEAAHG TVQRHYMQYL KGKKTSTNSI ASIFAWTRGL AHRGRLDGNE 

       370        380        390        400        410 
RLVKFANALE HACVRCVEKG IMTKDLYLLS KSPNGYVDTF EFLDAVKSEL DSELVNIA 

O14254 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 logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by kr flag YPRC Korea Mirror sites: Australia  Brazil  Canada  China  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!