ID   LEU3_CANGA              Reviewed;         365 AA.
AC   O14429; Q6FS35;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   16-JUN-2009, entry version 59.
DE   RecName: Full=3-isopropylmalate dehydrogenase;
DE            Short=3-IPM-DH;
DE            Short=IMDH;
DE            EC=1.1.1.85;
DE   AltName: Full=Beta-IPM dehydrogenase;
GN   Name=LEU2; OrderedLocusNames=CAGL0H03795g;
OS   Candida glabrata (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   mitosporic Nakaseomyces.
OX   NCBI_TaxID=5478;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65;
RA   Kitada K.;
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65;
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: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-
CC       methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-
CC       oxopentanoate. The product decarboxylates to 4-methyl-2
CC       oxopentanoate.
CC   -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-
CC       2-oxopentanoate + CO(2) + NADH.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC       similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 3/4.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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DR   EMBL; U90626; AAB62089.1; -; Genomic_DNA.
DR   EMBL; CR380954; CAG59892.1; -; Genomic_DNA.
DR   RefSeq; XP_446959.1; -.
DR   HSSP; P12010; 2AYQ.
DR   GeneID; 2888798; -.
DR   KEGG; cgr:CAGL0H03795g; -.
DR   HOGENOM; O14429; -.
DR   OMA; O14429; NTAFGLY.
DR   BRENDA; 1.1.1.85; 189220.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase 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:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR   InterPro; IPR004429; Isopropylmalate_DH.
DR   Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1.
DR   PANTHER; PTHR11835; IDH_IMDH_dimeric; 1.
DR   PANTHER; PTHR11835:SF13; IPMDH; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   TIGRFAMs; TIGR00169; leuB; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Cytoplasm; Leucine biosynthesis; Magnesium;
KW   Manganese; Metal-binding; NAD; Oxidoreductase.
FT   CHAIN         1    365       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083603.
FT   NP_BIND      80     91       NAD (By similarity).
FT   NP_BIND     290    301       NAD (By similarity).
FT   METAL       226    226       Magnesium or manganese (By similarity).
FT   METAL       251    251       Magnesium or manganese (By similarity).
FT   METAL       255    255       Magnesium or manganese (By similarity).
FT   BINDING      98     98       Substrate (By similarity).
FT   BINDING     108    108       Substrate (By similarity).
FT   BINDING     137    137       Substrate (By similarity).
FT   BINDING     226    226       Substrate (By similarity).
FT   SITE        144    144       Important for catalysis (By similarity).
FT   SITE        193    193       Important for catalysis (By similarity).
FT   CONFLICT     10     10       L -> P (in Ref. 1; AAB62089).
FT   CONFLICT     24     24       I -> N (in Ref. 1; AAB62089).
FT   CONFLICT     51     51       A -> P (in Ref. 1; AAB62089).
SQ   SEQUENCE   365 AA;  39305 MW;  05D59E0986360B82 CRC64;
     MAVTKTIVVL PGDHVGQEIT EEAIKVLNAI QECRPDKVNF KFDHHLIGGA AIDATGVPLP
     DEALEASKKA DAVLLGAVGG PKWGTGAVRP EQGLLKIRKE LQLYANLRPC NFASDSLLDL
     SPLKPEIARG TDFVVVRELV GGIYFGERKE DEGDGVAWDS EKYSVPEVQR ITRMAAFMAL
     QHNPPLPIWS LDKANVLASS RLWRKTVEET IKNEFPQLTV QHQLIDSAAM ILVKNPTHLN
     GIIITNNMFG DIISDEASVI PGSLGLLPSA SLASLPDKNT AFGLYEPCHG SAPDLPKGKV
     NPVATILSAA MMLKLSLDLF EEGEIIEQAV KKVLDSGIRT ADLKGTNSTT EVGDAVAKAV
     RELLA
//