ID   LEU3_CANMA              Reviewed;         373 AA.
AC   P07139;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   04-NOV-2008, entry version 61.
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;
OS   Candida maltosa (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   Candida.
OX   NCBI_TaxID=5479;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=88223465; PubMed=2897248; DOI=10.1007/BF00384606;
RA   Takagi M., Kobayashi N., Sugimoto M., Fujii T., Watari J., Yano K.;
RT   "Nucleotide sequencing analysis of a LEU gene of Candida maltosa which
RT   complements leuB mutation of Escherichia coli and leu2 mutation of
RT   Saccharomyces cerevisiae.";
RL   Curr. Genet. 11:451-457(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G587;
RX   MEDLINE=95163116; PubMed=7859302; DOI=10.1007/BF00309549;
RA   Becher D., Schulze S., Kasuske A., Schulze H., Samsonova I.A.,
RA   Oliver S.G.;
RT   "Molecular analysis of a leu2-mutant of Candida maltosa demonstrates
RT   the presence of multiple alleles.";
RL   Curr. Genet. 26:208-216(1994).
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; X05459; CAA29024.1; -; Genomic_DNA.
DR   EMBL; X72940; CAA51445.1; -; Genomic_DNA.
DR   PIR; S48228; S48228.
DR   HSSP; P12010; 2AYQ.
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:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR004429; 3-isopropylmalate_DHase.
DR   InterPro; IPR001804; IsoCit_IM_DHase.
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   Cytoplasm; Leucine biosynthesis; Magnesium; Manganese; Metal-binding;
KW   NAD; Oxidoreductase.
FT   CHAIN         1    373       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083604.
FT   NP_BIND      82     93       NAD (By similarity).
FT   NP_BIND     295    306       NAD (By similarity).
FT   METAL       231    231       Magnesium or manganese (By similarity).
FT   METAL       256    256       Magnesium or manganese (By similarity).
FT   METAL       260    260       Magnesium or manganese (By similarity).
FT   BINDING     100    100       Substrate (By similarity).
FT   BINDING     110    110       Substrate (By similarity).
FT   BINDING     139    139       Substrate (By similarity).
FT   BINDING     231    231       Substrate (By similarity).
FT   SITE        146    146       Important for catalysis (By similarity).
FT   SITE        198    198       Important for catalysis (By similarity).
SQ   SEQUENCE   373 AA;  40173 MW;  256E9886219BA529 CRC64;
     MSVKTKTITI LPGDHVGTEI VNEAIKVLEA IEAATPYQKI HFDFKHHLIG GAAIDATGVP
     LPDDALESAK NSDAVLLGAV GGPKWGTGAL RPEQGLLKIR KELNLYANIR PCNFASDSLL
     ELSPLRPEVV KGTNLIIVRE LVGGIYFGDR EEQEESADKQ TAWDTEKYTV DEVTRITRMA
     AFMALQHTPP LPIWSLDKAN VLASSRLWRR TVDKVISEEF PTLSVQHQLI DSAAMILIQN
     PTKLNGIIIT SNMFGDIISD EASVIPGSLG LLPSASLASL PDTNTAFGLY EPCHGSAPDL
     PANKVNPIAT ILSAASMLRL SLDCVKEAEA LEEAVKQVLD KGIRTADLRG TSSTTEVGDA
     IVEAVTKILK EKA
//