[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION. DOI=10.1021/bi00198a035; PubMed=8068643 [NCBI, ExPASy, EBI, Israel, Japan] Loftus T.M., Hall L.V., Anderson S.L., McAlister-Henn L.; "Isolation, characterization, and disruption of the yeast gene encoding cytosolic NADP-specific isocitrate dehydrogenase."; Biochemistry 33:9661-9667(1994).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; PubMed=9169871 [NCBI, ExPASy, EBI, Israel, Japan] Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."; Nature 387:87-90(1997).
[3]	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

FUNCTION: May function in the production of NADPH for fatty acid and sterol synthesis.
CATALYTIC ACTIVITY: Isocitrate + NADP⁺ = 2-oxoglutarate + CO₂ + NADPH.
CATALYTIC ACTIVITY: Oxalosuccinate + NADP⁺ = 2-oxoglutarate + CO₂ + NADPH.
COFACTOR: Binds 1 magnesium or manganese ion per subunit (By similarity).
ENZYME REGULATION: By catabolite repression.
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
PTM: The N-terminus is blocked.
MISCELLANEOUS: Present with 2620 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family.

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

L26312; AAA64516.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17246; AAB67464.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S51419; S51419.

RefSeq

NP_013275.1; -.

3D structure databases

HSSP

P33198; 1LWD. [HSSP ENTRY / PDB]

ModBase

P41939.

Protein-protein interaction databases

DIP

DIP:4252N; -.

IntAct

P41939; -.

Organism-specific databases

YLR174w; -.

S000004164; IDP2.

Gene expression databases

GermOnline

YLR174W; Saccharomyces cerevisiae.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from direct assay from SGD).
GO:0004450;	Molecular function: isocitrate dehydrogenase (NADP+) activity (inferred from electronic annotation from InterPro).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145;	Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006537;	Biological process: glutamate biosynthetic process (traceable author statement from SGD).
GO:0006097;	Biological process: glyoxylate cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0006102;	Biological process: isocitrate metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006099;	Biological process: tricarboxylic acid cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR004790; IsoCit_DHase_NADP-dep_euk.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.718.10; IDH_IMDH; 1.

PANTHER

PTHR11822; IDH_NADP_euk; 1.

Pfam

PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000108; IDH_NADP; 1.

TIGRFAMs

TIGR00127; nadp_idh_euk; 1.

PROSITE

PS00470; IDH_IMDH; 1.

ProtoNet

P41939.

Proteomic databases

PeptideAtlas

P41939; -.

Genome annotation databases

Ensembl

YLR174W; Saccharomyces cerevisiae. [Contig view]

850871; -.

Y13138_GR; YLR174W.

sce:YLR174W; -.

fig|4932.3.peg.4285; -.

Phylogenomic databases

HOGENOM

P41939; -.

Other

LinkHub

P41939; -.

NextBio

967206; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Direct protein sequencing; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP; Oxidoreductase; Tricarboxylic acid cycle.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 412`	`412`	`Isocitrate dehydrogenase [NADP] cytoplasmic.`	`PRO_0000083587`
`NP_BIND`	`75 77`	`3`	`NADP (By similarity).`
`NP_BIND`	`310 315`	`6`	`NADP (By similarity).`
`REGION`	`94 100`	`7`	`Substrate binding (By similarity).`
`METAL`	`252 252`		`Magnesium or manganese (By similarity).`
`METAL`	`275 275`		`Magnesium or manganese (By similarity).`
`BINDING`	`77 77`		`Substrate (By similarity).`
`BINDING`	`82 82`		`NADP (By similarity).`
`BINDING`	`109 109`		`Substrate (By similarity).`
`BINDING`	`132 132`		`Substrate (By similarity).`
`BINDING`	`260 260`		`NADP (By similarity).`
`BINDING`	`328 328`		`NADP; via amide nitrogen and carbonyl oxygen (By similarity).`
`SITE`	`139 139`	`1`	`Critical for catalysis (By similarity).`
`SITE`	`212 212`	`1`	`Critical for catalysis (By similarity).`
`CONFLICT`	`24 27`		`HLIR -> SFNQ (in Ref. 1; AAA64516).`
`CONFLICT`	`68 68`		`G -> R (in Ref. 1; AAA64516).`
`CONFLICT`	`185 185`		`T -> N (in Ref. 1; AAA64516).`
`CONFLICT`	`232 239`		`ARSYKEKF -> LEVIKRSL (in Ref. 1; AAA64516).`
`CONFLICT`	`267 267`		`I -> M (in Ref. 1; AAA64516).`
`CONFLICT`	`306 307`		`EA -> DR (in Ref. 1; AAA64516).`
`CONFLICT`	`316 323`		`FRQHQQGK -> LTDYDKGR (in Ref. 1; AAA64516).`

Sequence information

Length: 412 AA [This is the length of the unprocessed precursor]

Molecular weight: 46562 Da [This is the MW of the unprocessed precursor]

CRC64: 83EB54CC56A29857 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTKIKVANPI VEMDGDEQTR IIWHLIRDKL VLPYLDVDLK YYDLSVEYRD QTNDQVTVDS 

        70         80         90        100        110        120 
ATATLKYGVA VKCATITPDE ARVEEFHLKK MWKSPNGTIR NILGGTVFRE PIIIPRIPRL 

       130        140        150        160        170        180 
VPQWEKPIII GRHAFGDQYK ATDVIVPEEG ELRLVYKSKS GTHDVDLKVF DYPEHGGVAM 

       190        200        210        220        230        240 
MMYNTTDSIE GFAKASFELA IERKLPLYST TKNTILKKYD GKFKDVFEAM YARSYKEKFE 

       250        260        270        280        290        300 
SLGIWYEHRL IDDMVAQMLK SKGGYIIAMK NYDGDVESDI VAQGFGSLGL MTSVLITPDG 

       310        320        330        340        350        360 
KTFESEAAHG TVTRHFRQHQ QGKETSTNSI ASIFAWTRGI IQRGKLDNTP DVVKFGQILE 

       370        380        390        400        410 
SATVNTVQED GIMTKDLALI LGKSERSAYV TTEEFIDAVE SRLKKEFEAA AL

P41939 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools