ID IDH3A_CAEEL Reviewed; 358 AA. AC Q93714; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 13-APR-2004, sequence version 3. DT 27-MAR-2024, entry version 155. DE RecName: Full=Probable isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial; DE EC=1.1.1.41; DE AltName: Full=Isocitric dehydrogenase subunit alpha; DE AltName: Full=NAD(+)-specific ICDH subunit alpha; DE Flags: Precursor; GN Name=idha-1; ORFNames=F43G9.1; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). RN [2] {ECO:0000305} RP DISRUPTION PHENOTYPE. RX PubMed=35021096; DOI=10.1016/j.celrep.2021.110206; RA Yang R., Li Y., Wang Y., Zhang J., Fan Q., Tan J., Li W., Zou X., Liang B.; RT "NHR-80 senses the mitochondrial UPR to rewire citrate metabolism for lipid RT accumulation in Caenorhabditis elegans."; RL Cell Rep. 38:110206-110206(2022). CC -!- CATALYTIC ACTIVITY: CC Reaction=D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH; CC Xref=Rhea:RHEA:23632, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.41; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Heterooligomer of subunits alpha, beta, and gamma in the CC apparent ratio of 2:1:1. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes accumulation of CC citrate, leading to induction of the citrate-induced mitochondrial CC unfolded protein response (mtUPR). {ECO:0000269|PubMed:35021096}. CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z79755; CAB02111.2; -; Genomic_DNA. DR PIR; T22149; T22149. DR RefSeq; NP_492330.2; NM_059929.3. DR AlphaFoldDB; Q93714; -. DR SMR; Q93714; -. DR BioGRID; 38088; 29. DR IntAct; Q93714; 2. DR STRING; 6239.F43G9.1.2; -. DR iPTMnet; Q93714; -. DR EPD; Q93714; -. DR PaxDb; 6239-F43G9-1; -. DR PeptideAtlas; Q93714; -. DR EnsemblMetazoa; F43G9.1.1; F43G9.1.1; WBGene00009664. DR GeneID; 172655; -. DR KEGG; cel:CELE_F43G9.1; -. DR UCSC; F43G9.1.1; c. elegans. DR AGR; WB:WBGene00009664; -. DR WormBase; F43G9.1; CE34018; WBGene00009664; idha-1. DR eggNOG; KOG0785; Eukaryota. DR GeneTree; ENSGT00950000182989; -. DR HOGENOM; CLU_031953_0_0_1; -. DR InParanoid; Q93714; -. DR OMA; CVRPCRY; -. DR OrthoDB; 143577at2759; -. DR PhylomeDB; Q93714; -. DR Reactome; R-CEL-71403; Citric acid cycle (TCA cycle). DR PRO; PR:Q93714; -. DR Proteomes; UP000001940; Chromosome I. DR Bgee; WBGene00009664; Expressed in germ line (C elegans) and 4 other cell types or tissues. DR GO; GO:0005739; C:mitochondrion; HDA:WormBase. DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006102; P:isocitrate metabolic process; IBA:GO_Central. DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central. DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR004434; Isocitrate_DH_NAD. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR NCBIfam; TIGR00175; mito_nad_idh; 1. DR PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1. DR PANTHER; PTHR11835:SF34; ISOCITRATE DEHYDROGENASE [NAD] SUBUNIT ALPHA, MITOCHONDRIAL; 1. DR Pfam; PF00180; Iso_dh; 1. DR SMART; SM01329; Iso_dh; 1. DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1. DR PROSITE; PS00470; IDH_IMDH; 1. DR World-2DPAGE; 0020:Q93714; -. PE 3: Inferred from homology; KW Magnesium; Manganese; Metal-binding; Mitochondrion; NAD; Oxidoreductase; KW Reference proteome; Transit peptide; Tricarboxylic acid cycle. FT TRANSIT 1..? FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN ?..358 FT /note="Probable isocitrate dehydrogenase [NAD] subunit FT alpha, mitochondrial" FT /id="PRO_0000014441" FT BINDING 108 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 118 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 139 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 226 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P50213" FT BINDING 226 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 250 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P50213" FT BINDING 254 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P50213" FT SITE 146 FT /note="Critical for catalysis" FT /evidence="ECO:0000250" FT SITE 193 FT /note="Critical for catalysis" FT /evidence="ECO:0000250" SQ SEQUENCE 358 AA; 38466 MW; B175DC68C127610F CRC64; MLGKCIKKAS STVGQSIRYS SGDVRRVTLI PGDGIGPEIS ASVQKIFEAA DAPIAWDPVD VTPVKGRDGV FRIPSRCIEL MHANKVGLKG PLETPIGKGH RSLNLAVRKE FSLYANVRPC RSLEGHKTLY DNVDVVTIRE NTEGEYSGIE HEIVPGVVQS IKLITETASR NVASFAFEYA RQNGRKVVTA VHKANIMRQS DGLFLSICRE QAALYPDIKF KEAYLDTVCL NMVQDPSQYD VLVMPNLYGD ILSDLCAGLV GGLGVTPSGN IGKGAAVFES VHGTAPDIAG QDKANPTALL LSAVMMLRYM NLPQHAARIE KAVFDAIADG RAKTGDLGGT GTCSSFTADV CARVKDLE //