IDH1_KLULA
ID IDH1_KLULA Reviewed; 361 AA.
AC O94229;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=KLLA0F04103g;
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}.
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DR EMBL; AF045153; AAC69608.1; -; Genomic_DNA.
DR EMBL; CR382126; CAG97974.1; -; Genomic_DNA.
DR RefSeq; XP_455266.1; XM_455266.1.
DR AlphaFoldDB; O94229; -.
DR SMR; O94229; -.
DR STRING; 28985.XP_455266.1; -.
DR EnsemblFungi; CAG97974; CAG97974; KLLA0_F04103g.
DR GeneID; 2894997; -.
DR KEGG; kla:KLLA0_F04103g; -.
DR eggNOG; KOG0784; Eukaryota.
DR HOGENOM; CLU_031953_0_0_1; -.
DR InParanoid; O94229; -.
DR OMA; GTSMFEP; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0005962; C:mitochondrial isocitrate dehydrogenase complex (NAD+); IEA:EnsemblFungi.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
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..12
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 13..361
FT /note="Isocitrate dehydrogenase [NAD] subunit 1,
FT mitochondrial"
FT /id="PRO_0000014429"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P50213"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 148
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 195
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 361 AA; 39158 MW; 7F3D7F7C5406ECAB CRC64;
MLRQGIAAQK KSFATLAAEQ LLPKKYGGRY TVTLIPGDGV GKEVTDSVVK IFENENIPID
WETIDISGLE NTENVQRAVE SLKRNKVGLK GIWHTPADQT GHGSLNVALR KQLDIFANVA
LFKSIPGVKT RLNNIDMVII RENTEGEYSG LEHESVPGVV ESLKIMTRAK SERIARFAFD
FALKNNRKSV CAVHKANIMK LGDGLFRNTV NEIGANEYPE LDVKNIIVDN ASMQAVAKPH
QFDVLVTPNL YGSILGNIGS ALIGGPGLVP GANFGREYAV FEPGSRHVGL DIKGQNVANP
TAMILSSTLM LRHLGLNAYA DRISKATYDV ISEGKSTTRD IGGSASTSEF TNAVIEKLAK
L
