ID IDH1_YEAST Reviewed; 360 AA. AC P28834; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 2. DT 25-NOV-2008, entry version 75. DE RecName: Full=Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial; DE EC=1.1.1.41; DE AltName: Full=Isocitric dehydrogenase; DE AltName: Full=NAD(+)-specific ICDH; DE Flags: Precursor; GN Name=IDH1; OrderedLocusNames=YNL037C; ORFNames=N2690; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 49-61; RP 72-83; 325-333 AND 339-356. RX MEDLINE=92355609; PubMed=1644826; RA Cupp J.R., McAlister-Henn L.; RT "Cloning and characterization of the gene encoding the IDH1 subunit of RT NAD(+)-dependent isocitrate dehydrogenase from Saccharomyces RT cerevisiae."; RL J. Biol. Chem. 267:16417-16423(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX MEDLINE=97313269; PubMed=9169873; RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., RA Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., RA Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., RA Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., RA Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., RA Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., RA Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., RA Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., RA Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., RA Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., RA Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., RA Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., RA Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., RA Wambutt R., Wedler H., Zollner A., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV RT and its evolutionary implications."; RL Nature 387:93-98(1997). RN [3] RP PROTEIN SEQUENCE OF 12-27. RC STRAIN=SG7; RX MEDLINE=90330530; PubMed=2198251; RA Keys D.A., McAlister-Henn L.; RT "Subunit structure, expression, and function of NAD(H)-specific RT isocitrate dehydrogenase in Saccharomyces cerevisiae."; RL J. Bacteriol. 172:4280-4287(1990). RN [4] RP RNA-BINDING. RX MEDLINE=94089379; PubMed=7505425; DOI=10.1093/nar/21.23.5328; RA Elzinga S.D.J., Bednarz A.L., van Oosterum K., Dekker P.J.T., RA Grivell L.A.; RT "Yeast mitochondrial NAD(+)-dependent isocitrate dehydrogenase is an RT RNA-binding protein."; RL Nucleic Acids Res. 21:5328-5331(1993). RN [5] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). CC -!- FUNCTION: Performs an essential role in the oxidative function of CC the citric acid cycle. Also binds RNA; specifically to the 5'- CC untranslated leaders of mitochondrial mRNAs. CC -!- CATALYTIC ACTIVITY: Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) + CC NADH. CC -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By CC similarity). CC -!- ENZYME REGULATION: Allosterically regulated by several compounds CC including AMP, NAD+, and citrate. CC -!- SUBUNIT: Octamer of two non-identical subunits IDH1 and IDH2. CC -!- INTERACTION: CC P28241:IDH2; NbExp=2; IntAct=EBI-8878, EBI-8883; CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- MISCELLANEOUS: Present with 10500 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M95203; AAA34711.1; -; Genomic_DNA. DR EMBL; Z71313; CAA95904.1; -; Genomic_DNA. DR PIR; S31264; S31264. DR RefSeq; NP_014361.1; -. DR PDB; 3BLV; X-ray; 3.20 A; A/C/E/G=12-360. DR PDB; 3BLW; X-ray; 4.30 A; A/C/E/G/I/K/M/O=12-360. DR PDB; 3BLX; X-ray; 2.70 A; A/C/E/G/I/K/M/O=12-360. DR PDBsum; 3BLV; -. DR PDBsum; 3BLW; -. DR PDBsum; 3BLX; -. DR DIP; DIP:4376N; -. DR IntAct; P28834; -. DR PeptideAtlas; P28834; -. DR Ensembl; YNL037C; Saccharomyces cerevisiae. DR GeneID; 855691; -. DR GenomeReviews; Y13139_GR; YNL037C. DR KEGG; sce:YNL037C; -. DR NMPDR; fig|4932.3.peg.5438; -. DR CYGD; YNL037c; -. DR SGD; S000004982; IDH1. DR HOGENOM; P28834; -. DR BioCyc; MetaCyc:MON-13685; -. DR LinkHub; P28834; -. DR NextBio; 980007; -. DR ArrayExpress; P28834; -. DR GermOnline; YNL037C; Saccharomyces cerevisiae. DR GO; GO:0005962; C:mitochondrial isocitrate dehydrogenase comp...; IDA:SGD. DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD. DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006537; P:glutamate biosynthetic process; TAS:SGD. DR GO; GO:0006102; P:isocitrate metabolic process; TAS:SGD. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR InterPro; IPR004434; IsoCit_DHase_NAD_mit. DR InterPro; IPR001804; IsoCit_IM_DHase. DR Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1. DR PANTHER; PTHR11835; IDH_IMDH_dimeric; 1. DR Pfam; PF00180; Iso_dh; 1. DR TIGRFAMs; TIGR00175; mito_nad_idh; 1. DR PROSITE; PS00470; IDH_IMDH; 1. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; Complete proteome; KW Direct protein sequencing; Magnesium; Manganese; Metal-binding; KW Mitochondrion; NAD; Oxidoreductase; RNA-binding; Transit peptide; KW Tricarboxylic acid cycle. FT TRANSIT 1 11 Mitochondrion. FT CHAIN 12 360 Isocitrate dehydrogenase [NAD] subunit 1, FT mitochondrial. FT /FTId=PRO_0000014431. FT METAL 228 228 Magnesium or manganese (By similarity). FT BINDING 109 109 Substrate (By similarity). FT BINDING 140 140 Substrate (By similarity). FT BINDING 228 228 Substrate (By similarity). FT SITE 194 194 Critical for catalysis (By similarity). FT STRAND 29 34 FT TURN 37 39 FT HELIX 40 52 FT TURN 53 55 FT STRAND 57 62 FT HELIX 74 84 FT STRAND 85 89 FT HELIX 106 112 FT STRAND 116 122 FT STRAND 135 155 FT STRAND 158 166 FT HELIX 167 183 FT STRAND 188 193 FT TURN 195 197 FT HELIX 201 211 FT TURN 212 214 FT STRAND 220 226 FT HELIX 227 236 FT HELIX 238 240 FT STRAND 242 246 FT HELIX 248 261 FT STRAND 269 273 FT STRAND 278 284 FT HELIX 289 291 FT HELIX 300 312 FT HELIX 317 331 FT STRAND 332 335 FT HELIX 338 340 FT HELIX 346 357 SQ SEQUENCE 360 AA; 39324 MW; 0932E7B3CD685240 CRC64; MLNRTIAKRT LATAAQAERT LPKKYGGRFT VTLIPGDGVG KEITDSVRTI FEAENIPIDW ETINIKQTDH KEGVYEAVES LKRNKIGLKG LWHTPADQTG HGSLNVALRK QLDIYANVAL FKSLKGVKTR IPDIDLIVIR ENTEGEFSGL EHESVPGVVE SLKVMTRPKT ERIARFAFDF AKKYNRKSVT AVHKANIMKL GDGLFRNIIT EIGQKEYPDI DVSSIIVDNA SMQAVAKPHQ FDVLVTPSMY GTILGNIGAA LIGGPGLVAG ANFGRDYAVF EPGSRHVGLD IKGQNVANPT AMILSSTLML NHLGLNEYAT RISKAVHETI AEGKHTTRDI GGSSSTTDFT NEIINKLSTM //