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Database: UniProt
Entry: Q6CA33_YARLI
LinkDB: Q6CA33_YARLI
Original site: Q6CA33_YARLI 
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
//
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