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UniProtKB/Swiss-Prot entry P28834


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

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Entry information
Entry name IDH1_YEAST
Primary accession number P28834
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on July 1, 1993 (Sequence version 2)
Annotations were last modified on    October 14, 2008 (Entry version 73)
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
OrderedLocusNames: YNL037C
ORFNames: N2690
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 49-61; 72-83; 325-333 AND 339-356.
PubMed=1644826 [NCBI, ExPASy, EBI, Israel, Japan]
Cupp J.R., McAlister-Henn L.;
"Cloning and characterization of the gene encoding the IDH1 subunit of NAD(+)-dependent isocitrate dehydrogenase from Saccharomyces cerevisiae.";
J. Biol. Chem. 267:16417-16423(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873 [NCBI, ExPASy, EBI, Israel, Japan]
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications.";
Nature 387:93-98(1997).
[3]
PROTEIN SEQUENCE OF 12-27.
STRAIN=SG7;
PubMed=2198251 [NCBI, ExPASy, EBI, Israel, Japan]
Keys D.A., McAlister-Henn L.;
"Subunit structure, expression, and function of NAD(H)-specific isocitrate dehydrogenase in Saccharomyces cerevisiae.";
J. Bacteriol. 172:4280-4287(1990).
[4]
RNA-BINDING.
DOI=10.1093/nar/21.23.5328; PubMed=7505425 [NCBI, ExPASy, EBI, Israel, Japan]
Elzinga S.D.J., Bednarz A.L., van Oosterum K., Dekker P.J.T., Grivell L.A.;
"Yeast mitochondrial NAD(+)-dependent isocitrate dehydrogenase is an RNA-binding protein.";
Nucleic Acids Res. 21:5328-5331(1993).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
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
M95203; AAA34711.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z71313; CAA95904.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S31264; S31264.
RefSeq NP_014361.1; -.
3D structure databases
PDB
3BLV; X-ray; 3.20 A; A/C/E/G=12-360.[ExPASy / RCSB / EBI]
3BLW; X-ray; 4.30 A; A/C/E/G/I/K/M/O=12-360.[ExPASy / RCSB / EBI]
3BLX; X-ray; 2.70 A; A/C/E/G/I/K/M/O=12-360.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 3BLV; -.
3BLW; -.
3BLX; -.
ModBase P28834.
Protein-protein interaction databases
DIP DIP:4376N; -.
IntAct P28834; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-13685; -.
Organism-specific databases
CYGD YNL037c; -.
SGD S000004982; IDH1.
Yeast-GFP YNL037C.
Gene expression databases
ArrayExpress P28834; -.
GermOnline YNL037C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005962; Cellular component: mitochondrial isocitrate dehydrogenase complex (NAD+) (inferred from direct assay from SGD).
GO:0042645; Cellular component: mitochondrial nucleoid (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006537; Biological process: glutamate biosynthetic process (traceable author statement from SGD).
GO:0006102; Biological process: isocitrate metabolic process (traceable author statement from SGD).
GO:0006099; Biological process: tricarboxylic acid cycle (traceable author statement from SGD).
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 P28834.
Proteomic databases
PeptideAtlas P28834; -.
Genome annotation databases
Ensembl YNL037C; Saccharomyces cerevisiae. [Contig view]
GeneID 855691; -.
GenomeReviews Y13139_GR; YNL037C.
KEGG sce:YNL037C; -.
NMPDR fig|4932.3.peg.5438; -.
Phylogenomic databases
HOGENOM P28834; -.
Other
LinkHub P28834; -.
ProtoNet P28834.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Allosteric enzyme; Complete proteome; Direct protein sequencing; 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    11  11     Mitochondrion. 
CHAIN   12   360  349     Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial. PRO_0000014431
METAL   228   228        Magnesium or manganese (By similarity). 
BINDING   109   109        Substrate (By similarity). 
BINDING   140   140        Substrate (By similarity). 
BINDING   228   228        Substrate (By similarity). 
SITE   194   194  1     Critical for catalysis (By similarity). 
STRAND   29    34  6      
TURN   37    39  3      
HELIX   40    52  13      
TURN   53    55  3      
STRAND   57    62  6      
HELIX   74    84  11      
STRAND   85    89  5      
HELIX   106   112  7      
STRAND   116   122  7      
STRAND   135   155  21      
STRAND   158   166  9      
HELIX   167   183  17      
STRAND   188   193  6      
TURN   195   197  3      
HELIX   201   211  11      
TURN   212   214  3      
STRAND   220   226  7      
HELIX   227   236  10      
HELIX   238   240  3      
STRAND   242   246  5      
HELIX   248   261  14      
STRAND   269   273  5      
STRAND   278   284  7      
HELIX   289   291  3      
HELIX   300   312  13      
HELIX   317   331  15      
STRAND   332   335  4      
HELIX   338   340  3      
HELIX   346   357  12      
Sequence information
Length: 360 AA [This is the length of the unprocessed precursor] Molecular weight: 39324 Da [This is the MW of the unprocessed precursor] CRC64: 0932E7B3CD685240 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLNRTIAKRT LATAAQAERT LPKKYGGRFT VTLIPGDGVG KEITDSVRTI FEAENIPIDW 

        70         80         90        100        110        120 
ETINIKQTDH KEGVYEAVES LKRNKIGLKG LWHTPADQTG HGSLNVALRK QLDIYANVAL 

       130        140        150        160        170        180 
FKSLKGVKTR IPDIDLIVIR ENTEGEFSGL EHESVPGVVE SLKVMTRPKT ERIARFAFDF 

       190        200        210        220        230        240 
AKKYNRKSVT AVHKANIMKL GDGLFRNIIT EIGQKEYPDI DVSSIIVDNA SMQAVAKPHQ 

       250        260        270        280        290        300 
FDVLVTPSMY GTILGNIGAA LIGGPGLVAG ANFGRDYAVF EPGSRHVGLD IKGQNVANPT 

       310        320        330        340        350        360 
AMILSSTLML NHLGLNEYAT RISKAVHETI AEGKHTTRDI GGSSSTTDFT NEIINKLSTM 

P28834 in FASTA format

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