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   16-JUN-2009, entry version 59.
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 (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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF045153; AAC69608.1; -; Genomic_DNA.
DR   EMBL; CR382126; CAG97974.1; -; Genomic_DNA.
DR   RefSeq; XP_455266.1; -.
DR   HSSP; P00351; 1XAA.
DR   GeneID; 2894997; -.
DR   KEGG; kla:KLLA0F04103g; -.
DR   HOGENOM; O94229; -.
DR   OMA; O94229; NVALRKQ.
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     12       Mitochondrion (By similarity).
FT   CHAIN        13    361       Isocitrate dehydrogenase [NAD] subunit 1,
FT                                mitochondrial.
FT                                /FTId=PRO_0000014429.
FT   METAL       229    229       Magnesium or manganese (By similarity).
FT   BINDING     110    110       Substrate (By similarity).
FT   BINDING     141    141       Substrate (By similarity).
FT   BINDING     229    229       Substrate (By similarity).
FT   SITE        148    148       Critical for catalysis (By similarity).
FT   SITE        195    195       Critical for catalysis (By similarity).
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
//