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P53982 (IDHH_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isocitrate dehydrogenase [NADP]
Short name=IDH
EC=1.1.1.42
Alternative name(s):
IDP
NADP(+)-specific ICDH
Oxalosuccinate decarboxylase
Gene names
Name:IDP3
Ordered Locus Names:YNL009W
ORF Names:N2870
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May function in the production of NADPH for fatty acid and sterol synthesis.

Catalytic activity

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

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420Isocitrate dehydrogenase [NADP]
PRO_0000083588

Regions

Nucleotide binding75 – 773NADP By similarity
Nucleotide binding310 – 3156NADP By similarity
Region94 – 1007Substrate binding By similarity

Sites

Metal binding2521Magnesium or manganese By similarity
Metal binding2751Magnesium or manganese By similarity
Binding site771Substrate By similarity
Binding site821NADP By similarity
Binding site1091Substrate By similarity
Binding site1321Substrate By similarity
Binding site2601NADP By similarity
Binding site3281NADP; via amide nitrogen and carbonyl oxygen By similarity
Site1391Critical for catalysis By similarity
Site2121Critical for catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
P53982 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 4094007E13FCD506

FASTA42047,856
        10         20         30         40         50         60 
MSKIKVVHPI VEMDGDEQTR VIWKLIKEKL ILPYLDVDLK YYDLSIQERD RTNDQVTKDS 

        70         80         90        100        110        120 
SYATLKYGVA VKCATITPDE ARMKEFNLKE MWKSPNGTIR NILGGTVFRE PIIIPKIPRL 

       130        140        150        160        170        180 
VPHWEKPIII GRHAFGDQYR ATDIKIKKAG KLRLQFSSDD GKENIDLKVY EFPKSGGIAM 

       190        200        210        220        230        240 
AMFNTNDSIK GFAKASFELA LKRKLPLFFT TKNTILKNYD NQFKQIFDNL FDKEYKEKFQ 

       250        260        270        280        290        300 
ALKITYEHRL IDDMVAQMLK SKGGFIIAMK NYDGDVQSDI VAQGFGSLGL MTSILITPDG 

       310        320        330        340        350        360 
KTFESEAAHG TVTRHFRKHQ RGEETSTNSI ASIFAWTRAI IQRGKLDNTD DVIKFGNLLE 

       370        380        390        400        410        420 
KATLDTVQVG GKMTKDLALM LGKTNRSSYV TTEEFIDEVA KRLQNMMLSS NEDKKGMCKL

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z71285 Genomic DNA. Translation: CAA95869.1.
AY693154 Genomic DNA. Translation: AAT93173.1.
BK006947 Genomic DNA. Translation: DAA10534.1.
PIRS62921.
RefSeqNP_014389.3. NM_001182848.3.

3D structure databases

ProteinModelPortalP53982.
SMRP53982. Positions 2-404.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35816. 30 interactions.
DIPDIP-4693N.
IntActP53982. 4 interactions.
MINTMINT-473180.
STRING4932.YNL009W.

Proteomic databases

PaxDbP53982.
PeptideAtlasP53982.
PRIDEP53982.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL009W; YNL009W; YNL009W.
GeneID855723.
KEGGsce:YNL009W.

Organism-specific databases

CYGDYNL009w.
SGDS000004954. IDP3.

Phylogenomic databases

eggNOGCOG0538.
GeneTreeENSGT00390000012547.
HOGENOMHOG000019858.
KOK00031.
OMAPHWEKPI.
OrthoDBEOG7G4QQD.

Enzyme and pathway databases

BioCycYEAST:YNL009W-MONOMER.
SABIO-RKP53982.

Gene expression databases

GenevestigatorP53982.

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

NextBio980090.

Entry information

Entry nameIDHH_YEAST
AccessionPrimary (citable) accession number: P53982
Secondary accession number(s): D6W1G8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 112 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 XIV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents