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   16-JUN-2009, entry version 59.
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 (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=28985;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC MYA-539 / JBD100;
RX   MEDLINE=20426969; PubMed=10975257; DOI=10.1007/s002940000132;
RA   Elzinga S.D.J., van Oosterum K., Maat C., Grivell L.A.,
RA   van der Spek H.;
RT   "Isolation and RNA-binding analysis of NAD+ -isocitrate dehydrogenases
RT   from 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 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., 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   -!- FUNCTION: Performs an essential role in the oxidative function of
CC       the citric acid cycle (By similarity).
CC   -!- CATALYTIC ACTIVITY: Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) +
CC       NADH.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC       similarity).
CC   -!- SUBUNIT: Octamer of two non-identical subunits IDH1 and IDH2 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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DR   EMBL; AF045154; AAC69609.1; -; Genomic_DNA.
DR   EMBL; CR382125; CAG99173.1; -; Genomic_DNA.
DR   RefSeq; XP_454086.1; -.
DR   HSSP; P00351; 1XAA.
DR   GeneID; 2894289; -.
DR   KEGG; kla:KLLA0E03058g; -.
DR   HOGENOM; O94230; -.
DR   OMA; O94230; GGNSKCS.
DR   BRENDA; 1.1.1.41; 74088.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR   InterPro; IPR004434; Isocitrate_DH_NAD_mit.
DR   Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1.
DR   PANTHER; PTHR11835; IDH_IMDH_dimeric; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   TIGRFAMs; TIGR00175; mito_nad_idh; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW   NAD; Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT       1     14       Mitochondrion (By similarity).
FT   CHAIN        15    368       Isocitrate dehydrogenase [NAD] subunit 2,
FT                                mitochondrial.
FT                                /FTId=PRO_0000014432.
FT   METAL       236    236       Magnesium or manganese (By similarity).
FT   METAL       262    262       Magnesium or manganese (By similarity).
FT   METAL       266    266       Magnesium or manganese (By similarity).
FT   BINDING     118    118       Substrate (By similarity).
FT   BINDING     128    128       Substrate (By similarity).
FT   BINDING     149    149       Substrate (By similarity).
FT   BINDING     236    236       Substrate (By similarity).
FT   SITE        156    156       Critical for catalysis (By similarity).
FT   SITE        203    203       Critical for catalysis (By similarity).
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
//