IDH2_KLULA
ID IDH2_KLULA Reviewed; 368 AA.
AC O94230;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial;
DE EC=1.1.1.41;
DE AltName: Full=Isocitric dehydrogenase;
DE AltName: Full=NAD(+)-specific ICDH;
DE Flags: Precursor;
GN Name=IDH2; OrderedLocusNames=KLLA0E03058g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC MYA-539 / JBD100;
RX PubMed=10975257; DOI=10.1007/s002940000132;
RA Elzinga S.D.J., van Oosterum K., Maat C., Grivell L.A., van der Spek H.;
RT "Isolation and RNA-binding analysis of NAD+ -isocitrate dehydrogenases from
RT Kluyveromyces lactis and Schizosaccharomyces pombe.";
RL Curr. Genet. 38:87-94(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Performs an essential role in the oxidative function of the
CC citric acid cycle. {ECO:0000250}.
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: Octamer of two non-identical subunits IDH1 and IDH2.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
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; AF045154; AAC69609.1; -; Genomic_DNA.
DR EMBL; CR382125; CAG99173.1; -; Genomic_DNA.
DR RefSeq; XP_454086.1; XM_454086.1.
DR AlphaFoldDB; O94230; -.
DR SMR; O94230; -.
DR STRING; 28985.XP_454086.1; -.
DR EnsemblFungi; CAG99173; CAG99173; KLLA0_E03125g.
DR GeneID; 2894289; -.
DR KEGG; kla:KLLA0_E03125g; -.
DR eggNOG; KOG0785; Eukaryota.
DR HOGENOM; CLU_031953_0_1_1; -.
DR InParanoid; O94230; -.
DR OMA; CVRPCRY; -.
DR Proteomes; UP000000598; Chromosome E.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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..14
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 15..368
FT /note="Isocitrate dehydrogenase [NAD] subunit 2,
FT mitochondrial"
FT /id="PRO_0000014432"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P50213"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P50213"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P50213"
FT SITE 156
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 203
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 368 AA; 39579 MW; E6BFAE7F676F5FB6 CRC64;
MFRQSIVKQS CRFLATKKQP SIGRYTGKPN PKTGKYTVSF IEGDGVGPEI SKSVKAIFSA
AKVPIEWESC DVSPIFVNGL TTIPDPAVAS INKNLIALKG PLATPIGKGH RSLNLTLRKT
FGLFANVRPA KSIEGYKTTY ENVNLVLIRE NTEGEYSGIE HVVAPGVVQS IKLITQDASE
RVIRYAFEYA RAVDRSKVLV VHKSTIQRLA DGLFVDVAKK LSSEYPDIEL QTELLDNTVL
KTVQHPEAYD DVVVVCPNLY GDILSDLNSG LSAGSLGLTP SANIGHTVSI FEAVHGSAPD
IAGQNKANPT ALLLSSVMML NHMGLTEHAD KIEKAVLTTI ASDAKNRTGD LGGSASTSSF
TDAVIERL
