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P28834 (IDH1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial

EC=1.1.1.41
Alternative name(s):
Isocitric dehydrogenase
NAD(+)-specific ICDH
Gene names
Name:IDH1
Ordered Locus Names:YNL037C
ORF Names:N2690
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Performs an essential role in the oxidative function of the citric acid cycle. Also binds RNA; specifically to the 5'-untranslated leaders of mitochondrial mRNAs.

Catalytic activity

Isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH.

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Enzyme regulation

Allosterically regulated by several compounds including AMP, NAD+, and citrate.

Subunit structure

Octamer of two non-identical subunits IDH1 and IDH2.

Subcellular location

Mitochondrion.

Miscellaneous

Present with 10500 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IDH2P282417EBI-8878,EBI-8883

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1111Mitochondrion Ref.4
Chain12 – 360349Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial
PRO_0000014431

Sites

Metal binding2281Magnesium or manganese By similarity
Binding site1091Substrate By similarity
Binding site1401Substrate By similarity
Binding site2281Substrate By similarity
Site1941Critical for catalysis By similarity

Secondary structure

.......................................................... 360
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P28834 [UniParc].

Last modified July 1, 1993. Version 2.
Checksum: 0932E7B3CD685240

FASTA36039,324
        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 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the gene encoding the IDH1 subunit of NAD(+)-dependent isocitrate dehydrogenase from Saccharomyces cerevisiae."
Cupp J.R., McAlister-Henn L.
J. Biol. Chem. 267:16417-16423(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 49-61; 72-83; 325-333 AND 339-356.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
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. expand/collapse author list , 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.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Subunit structure, expression, and function of NAD(H)-specific isocitrate dehydrogenase in Saccharomyces cerevisiae."
Keys D.A., McAlister-Henn L.
J. Bacteriol. 172:4280-4287(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 12-27.
Strain: SG7.
[5]"Yeast mitochondrial NAD(+)-dependent isocitrate dehydrogenase is an RNA-binding protein."
Elzinga S.D.J., Bednarz A.L., van Oosterum K., Dekker P.J.T., Grivell L.A.
Nucleic Acids Res. 21:5328-5331(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING.
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M95203 Genomic DNA. Translation: AAA34711.1.
Z71313 Genomic DNA. Translation: CAA95904.1.
BK006947 Genomic DNA. Translation: DAA10508.1.
PIRS31264.
RefSeqNP_014361.1. NM_001182876.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BLVX-ray3.20A/C/E/G12-360[»]
3BLWX-ray4.30A/C/E/G/I/K/M/O12-360[»]
3BLXX-ray2.70A/C/E/G/I/K/M/O12-360[»]
ProteinModelPortalP28834.
SMRP28834. Positions 28-360.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4376N.
IntActP28834. 17 interactions.
MINTMINT-484546.
STRING4932.YNL037C.

Proteomic databases

PaxDbP28834.
PeptideAtlasP28834.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL037C; YNL037C; YNL037C.
GeneID855691.
KEGGsce:YNL037C.

Organism-specific databases

CYGDYNL037c.
SGDS000004982. IDH1.

Phylogenomic databases

eggNOGCOG0473.
GeneTreeENSGT00590000083091.
HOGENOMHOG000021113.
KOK00030.
OMAARFAFDF.
OrthoDBEOG473T12.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13685.
YEAST:YNL037C-MONOMER.
ReactomeREACT_118590. Mitochondrial Protein Import (yeast).
REACT_85873. Metabolism of proteins.

Gene expression databases

GenevestigatorP28834.
GermOnlineYNL037C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR004434. Isocitrate_DH_NAD.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERPTHR11835. PTHR11835. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR00175. mito_nad_idh. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP28834.
NextBio980007.

Entry information

Entry nameIDH1_YEAST
AccessionPrimary (citable) accession number: P28834
Secondary accession number(s): D6W1E2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: July 1, 1993
Last modified: May 29, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families