ID Q6CA33_YARLI Unreviewed; 369 AA.
AC Q6CA33;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 24-JAN-2024, entry version 108.
DE RecName: Full=isocitrate dehydrogenase (NAD(+)) {ECO:0000256|ARBA:ARBA00013012};
DE EC=1.1.1.41 {ECO:0000256|ARBA:ARBA00013012};
DE AltName: Full=Isocitric dehydrogenase {ECO:0000256|ARBA:ARBA00030683};
DE AltName: Full=NAD(+)-specific ICDH {ECO:0000256|ARBA:ARBA00030631};
GN ORFNames=YALI0_D06303g {ECO:0000313|EMBL:CAG80667.1};
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG80667.1, ECO:0000313|Proteomes:UP000001300};
RN [1] {ECO:0000313|EMBL:CAG80667.1, ECO:0000313|Proteomes:UP000001300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
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., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 Evidence={ECO:0000256|ARBA:ARBA00000837};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: Octamer of two non-identical subunits IDH1 and IDH2.
CC {ECO:0000256|ARBA:ARBA00011567}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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DR EMBL; CR382130; CAG80667.1; -; Genomic_DNA.
DR RefSeq; XP_502479.1; XM_502479.1.
DR AlphaFoldDB; Q6CA33; -.
DR STRING; 284591.Q6CA33; -.
DR EnsemblFungi; CAG80667; CAG80667; YALI0_D06303g.
DR GeneID; 2910868; -.
DR KEGG; yli:YALI0D06303g; -.
DR VEuPathDB; FungiDB:YALI0_D06303g; -.
DR HOGENOM; CLU_031953_0_1_1; -.
DR InParanoid; Q6CA33; -.
DR OMA; CVRPCRY; -.
DR OrthoDB; 143577at2759; -.
DR Proteomes; UP000001300; Chromosome D.
DR GO; GO:0005962; C:mitochondrial isocitrate dehydrogenase complex (NAD+); IEA:EnsemblFungi.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001300};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 38..364
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 369 AA; 40003 MW; ADA1C3D8014EB369 CRC64;
MLNLRTALRA VRPVTLTRSY ATSVASFTGQ KNSNGKYTVS LIEGDGIGTE ISKAVKDIYH
AAKVPIDWEV VDVTPTLVNG KTTIPDSAIE SINRNKVALK GPLATPIGKG HVSMNLTLRR
TFNLFANVRP CKSVVGYKTP YENVDTLLIR ENTEGEYSGI EHTVVPGVVQ SIKLITREAS
ERVIRYAYEY ALSRGMKKVL VVHKASIMKV SDGLFLEVAR ELAKEYPSID LSVELIDNTC
LRMVQDPALY RDVVMVMPNL YGDILSDLAS GLIGGLGLTP SGNMGDEVSI FEAVHGSAPD
IAGKGLANPT ALLLSSVMML RHMGLNDNAT NIEQAVFGTI ASGPENRTKD LKGTATTSHF
AEQIIKRLK
//