IDH3B_CAEEL
ID IDH3B_CAEEL Reviewed; 379 AA.
AC Q93353;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Probable isocitrate dehydrogenase [NAD] subunit beta, mitochondrial;
DE EC=1.1.1.41;
DE AltName: Full=Isocitric dehydrogenase subunit beta;
DE AltName: Full=NAD(+)-specific ICDH subunit beta;
DE Flags: Precursor;
GN Name=idhb-1; ORFNames=C37E2.1;
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; Z81046; CAB02822.1; -; Genomic_DNA.
DR PIR; T19810; T19810.
DR RefSeq; NP_510362.1; NM_077961.5.
DR AlphaFoldDB; Q93353; -.
DR SMR; Q93353; -.
DR BioGRID; 46427; 7.
DR DIP; DIP-27476N; -.
DR IntAct; Q93353; 1.
DR STRING; 6239.C37E2.1.1; -.
DR EPD; Q93353; -.
DR PaxDb; Q93353; -.
DR PeptideAtlas; Q93353; -.
DR EnsemblMetazoa; C37E2.1.1; C37E2.1.1; WBGene00007993.
DR EnsemblMetazoa; C37E2.1.2; C37E2.1.2; WBGene00007993.
DR GeneID; 181528; -.
DR KEGG; cel:CELE_C37E2.1; -.
DR UCSC; C37E2.1.2; c. elegans.
DR CTD; 181528; -.
DR WormBase; C37E2.1; CE08620; WBGene00007993; idhb-1.
DR eggNOG; KOG0784; Eukaryota.
DR GeneTree; ENSGT00950000182989; -.
DR HOGENOM; CLU_031953_0_1_1; -.
DR InParanoid; Q93353; -.
DR OMA; TCAHKAN; -.
DR OrthoDB; 868374at2759; -.
DR PhylomeDB; Q93353; -.
DR Reactome; R-CEL-71403; Citric acid cycle (TCA cycle).
DR PRO; PR:Q93353; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00007993; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005962; C:mitochondrial isocitrate dehydrogenase complex (NAD+); IEA:UniProt.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
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..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 32..379
FT /note="Probable isocitrate dehydrogenase [NAD] subunit
FT beta, mitochondrial"
FT /id="PRO_0000014448"
FT BINDING 44..72
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P50213"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 168
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 215
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 379 AA; 41553 MW; F099425960AB3086 CRC64;
MLSRTVSSLS RVAPQTLGAV NAASSRQYSI TAPRPPTELN QKLKVTIIPG DGVGPELIYT
VQDIVKQTGI PIEFEEIFLS EVHYTRSSSI ENAVESIGRN NNVALKGAIE ESAVLHTEGE
LQGLNMRLRR SLDLFANVVH IKTLDGIKTR HGKQLDFVIV REQTEGEYSS LEHELVPGVI
ECLKISTRTK AERIAKFAFD YATKTGRKKV TAVHKANIMK LGDGLFLRTC EGVAKQYPKI
QFESMIIDNT CMQLVSKPEQ FDVMVMPNLY GNIIDNLAAG LVGGAGVVPG QSVGRDFVIF
EPGSRHSFQE AMGRSIANPT AMILCAANML NHLHLDAWGN SLRQAVADVV KEGKVRTRDL
GGYATTVDFA DAVIDKFRI
