IDH3A_CAEEL
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 03-AUG-2022, entry version 148.
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).
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 -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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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; 27.
DR IntAct; Q93714; 2.
DR STRING; 6239.F43G9.1; -.
DR iPTMnet; Q93714; -.
DR World-2DPAGE; 0020:Q93714; -.
DR EPD; Q93714; -.
DR PaxDb; Q93714; -.
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 CTD; 172655; -.
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; 868374at2759; -.
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 tissues.
DR GO; GO:0005962; C:mitochondrial isocitrate dehydrogenase complex (NAD+); IEA:UniProt.
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 InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004434; Isocitrate_DH_NAD.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00175; mito_nad_idh; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
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
