Reviewed, UniProtKB/Swiss-Prot P53982 (IDHH_YEAST)

Names and origin

Protein names

Recommended name:
    Isocitrate dehydrogenase [NADP]
      Short name=IDH
    EC=1.1.1.42
Alternative name(s):
    Oxalosuccinate decarboxylase
    NADP(+)-specific ICDH
    IDP

Gene names

Name:	IDP3
Ordered Locus Names:	YNL009W
ORF Names:	N2870

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	420 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 + CO(2) + NADPH. Oxalosuccinate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH.
Cofactor	Binds 1 magnesium or manganese ion per subunit By similarity.
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Ontologies

Keywords
Biological process	Glyoxylate bypass Tricarboxylic acid cycle
Ligand	Magnesium Manganese Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	NADPH regeneration Traceable author statement. Source: SGD fatty acid beta-oxidation Inferred from mutant phenotype. Source: SGD glyoxylate cycle Inferred from electronic annotation. Source: UniProtKB-KW isocitrate metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from direct assay. Source: SGD peroxisome Inferred from direct assay. Source: SGD
Molecular function	isocitrate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRP40	P33203	1	EBI-8892,EBI-701
RSP5	P39940	1	EBI-8892,EBI-16219
SSM4	P40318	1	EBI-8892,EBI-18208

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 420	420	Isocitrate dehydrogenase [NADP]		PRO_0000083588
Regions
	Nucleotide binding	75 – 77	3	NADP By similarity
	Nucleotide binding	310 – 315	6	NADP By similarity
	Region	94 – 100	7	Substrate binding By similarity
Sites
	Metal binding	252	1	Magnesium or manganese By similarity
	Metal binding	275	1	Magnesium or manganese By similarity
	Binding site	77	1	Substrate By similarity
	Binding site	82	1	NADP By similarity
	Binding site	109	1	Substrate By similarity
	Binding site	132	1	Substrate By similarity
	Binding site	260	1	NADP By similarity
	Binding site	328	1	NADP; via amide nitrogen and carbonyl oxygen By similarity
	Site	139	1	Critical for catalysis By similarity
	Site	212	1	Critical for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	P53982-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 4094007E13FCD506	FASTA	420	47,856
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"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. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z71285 Genomic DNA. Translation: CAA95869.1. AY693154 Genomic DNA. Translation: AAT93173.1.
PIR	S62921.
RefSeq	NP_014389.1.
3D structure databases
HSSP	HSSP built from PDB template 1LWD based on UniProtKB P33198.
SMR	P53982. Positions 3-407.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4693N.
IntAct	P53982.
Proteomic databases
PeptideAtlas	P53982.
Genome annotation databases
Ensembl	YNL009W. Saccharomyces cerevisiae. [Contig view]
GeneID	855723.
GenomeReviews	Gene locus YNL009W in contig Y13139_GR.
KEGG	sce:YNL009W.
NMPDR	fig|4932.3.peg.5467.
Organism-specific databases
CYGD	YNL009w.
SGD	S000004954. IDP3.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P53982.
Gene expression databases
GermOnline	YNL009W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004790. IsoCit_DHase_NADP-dep_euk. IPR001804. IsoCit_IM_DHase. [Graphical view]
Gene3D	G3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHER	PTHR11822. IDH_NADP_euk. 1 hit.
Pfam	PF00180. Iso_dh. 1 hit. [Graphical view]
PIRSF	PIRSF000108. IDH_NADP. 1 hit.
TIGRFAMs	TIGR00127. nadp_idh_euk. 1 hit.
PROSITE	PS00470. IDH_IMDH. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
LinkHub	P53982.
NextBio	980090.

Entry information

Entry name

IDHH_YEAST

Accession

Primary (citable) accession number: P53982

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 25, 2008
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)