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P21954 (IDHP_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isocitrate dehydrogenase [NADP], mitochondrial

Short name=IDH
EC=1.1.1.42
Alternative name(s):
IDP
NADP(+)-specific ICDH
Oxalosuccinate decarboxylase
Gene names
Name:IDP1
Ordered Locus Names:YDL066W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mitochondrial IDP1 may regulate flux through the tricarboxylic acid cycle and respiration. Its probably critical function is the production of NADPH.

Catalytic activity

Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH.

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Enzyme regulation

The enzyme is subject to end product inhibition by NADPH and 2-oxoglutarate.

Subunit structure

Homodimer.

Subcellular location

Mitochondrion.

Induction

By growth with glucose as a carbon source.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KAR2P164742EBI-8898,EBI-7876

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1616Mitochondrion Ref.1
Chain17 – 428412Isocitrate dehydrogenase [NADP], mitochondrial
PRO_0000014426

Regions

Nucleotide binding91 – 933NADP By similarity
Nucleotide binding327 – 3326NADP By similarity
Region110 – 1167Substrate binding By similarity

Sites

Metal binding2691Magnesium or manganese By similarity
Metal binding2921Magnesium or manganese By similarity
Binding site931Substrate By similarity
Binding site981NADP By similarity
Binding site1251Substrate By similarity
Binding site1481Substrate By similarity
Binding site2771NADP By similarity
Binding site3451NADP; via amide nitrogen and carbonyl oxygen By similarity
Site1551Critical for catalysis By similarity
Site2291Critical for catalysis By similarity

Secondary structure

................................................................... 428
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21954 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 7F885785B8682416

FASTA42848,190
        10         20         30         40         50         60 
MSMLSRRLFS TSRLAAFSKI KVKQPVVELD GDEMTRIIWD KIKKKLILPY LDVDLKYYDL 

        70         80         90        100        110        120 
SVESRDATSD KITQDAAEAI KKYGVGIKCA TITPDEARVK EFNLHKMWKS PNGTIRNILG 

       130        140        150        160        170        180 
GTVFREPIVI PRIPRLVPRW EKPIIIGRHA HGDQYKATDT LIPGPGSLEL VYKPSDPTTA 

       190        200        210        220        230        240 
QPQTLKVYDY KGSGVAMAMY NTDESIEGFA HSSFKLAIDK KLNLFLSTKN TILKKYDGRF 

       250        260        270        280        290        300 
KDIFQEVYEA QYKSKFEQLG IHYEHRLIDD MVAQMIKSKG GFIMALKNYD GDVQSDIVAQ 

       310        320        330        340        350        360 
GFGSLGLMTS ILVTPDGKTF ESEAAHGTVT RHYRKYQKGE ETSTNSIASI FAWSRGLLKR 

       370        380        390        400        410        420 
GELDNTPALC KFANILESAT LNTVQQDGIM TKDLALACGN NERSAYVTTE EFLDAVEKRL 


QKEIKSIE 

« Hide

References

« Hide 'large scale' references
[1]"Isolation, nucleotide sequence, and disruption of the Saccharomyces cerevisiae gene encoding mitochondrial NADP(H)-specific isocitrate dehydrogenase."
Haselbeck R.J., McAlister-Henn L.
J. Biol. Chem. 266:2339-2345(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 17-36.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M57229 Genomic DNA. Translation: AAA34703.1.
Z74114 Genomic DNA. Translation: CAA98631.1.
BK006938 Genomic DNA. Translation: DAA11791.1.
PIRDCBYIS. A38610.
RefSeqNP_010217.1. NM_001180125.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QFVX-ray2.30A/B/C/D16-428[»]
2QFWX-ray2.60A/B/C/D/E/F16-428[»]
2QFXX-ray2.70A/B/C/D/E/F16-428[»]
2QFYX-ray2.10A/B/C/D/E/F16-428[»]
ProteinModelPortalP21954.
SMRP21954. Positions 17-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31993. 40 interactions.
DIPDIP-4494N.
IntActP21954. 18 interactions.
MINTMINT-510681.
STRING4932.YDL066W.

Proteomic databases

PaxDbP21954.
PeptideAtlasP21954.
PRIDEP21954.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL066W; YDL066W; YDL066W.
GeneID851493.
KEGGsce:YDL066W.

Organism-specific databases

CYGDYDL066w.
SGDS000002224. IDP1.

Phylogenomic databases

eggNOGCOG0538.
GeneTreeENSGT00390000012547.
HOGENOMHOG000019858.
KOK00031.
OMAMTRDDWV.
OrthoDBEOG7G4QQD.

Enzyme and pathway databases

BioCycYEAST:YDL066W-MONOMER.
SABIO-RKP21954.

Gene expression databases

GenevestigatorP21954.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR004790. Isocitrate_DH_NADP.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERPTHR11822. PTHR11822. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000108. IDH_NADP. 1 hit.
TIGRFAMsTIGR00127. nadp_idh_euk. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP21954.
NextBio968825.
PROP21954.

Entry information

Entry nameIDHP_YEAST
AccessionPrimary (citable) accession number: P21954
Secondary accession number(s): D6VRT1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: April 16, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references