ID   LEU3_ARXAD              Reviewed;         362 AA.
AC   Q8NKB8;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-NOV-2008, entry version 34.
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   Arxula adeninivorans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Dipodascaceae;
OC   mitosporic Dipodascaceae; Arxula.
OX   NCBI_TaxID=37620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LS3;
RX   MEDLINE=22588491; PubMed=12702456; DOI=10.1016/S1567-1356(02)00190-3;
RA   Wartmann T., Stoltenburg R., Boeer E., Sieber H., Bartelsen O.,
RA   Gellissen G., Kunze G.;
RT   "The ALEU2 gene -- a new component for an Arxula adeninivorans-based
RT   expression platform.";
RL   FEMS Yeast Res. 3:223-232(2003).
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; AJ488496; CAD32688.1; -; Genomic_DNA.
DR   HSSP; P12010; 2AYQ.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:InterPro.
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:0009098; P:leucine biosynthetic process; IEA:InterPro.
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    362       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083597.
FT   NP_BIND      77     88       NAD (By similarity).
FT   NP_BIND     287    298       NAD (By similarity).
FT   METAL       223    223       Magnesium or manganese (By similarity).
FT   METAL       248    248       Magnesium or manganese (By similarity).
FT   METAL       252    252       Magnesium or manganese (By similarity).
FT   BINDING      95     95       Substrate (By similarity).
FT   BINDING     105    105       Substrate (By similarity).
FT   BINDING     134    134       Substrate (By similarity).
FT   BINDING     223    223       Substrate (By similarity).
FT   SITE        141    141       Important for catalysis (By similarity).
FT   SITE        190    190       Important for catalysis (By similarity).
SQ   SEQUENCE   362 AA;  38833 MW;  AB9CD5FC4CD71DB6 CRC64;
     MSKNIIILSG DHVGPEVTAE AIKVLEAITQ ARPNVKFNFD HKLIGGAAID ATGSPLPDET
     LEASKKADAV LLGAVGGPKW GTGAVRPEQG LLKIRKELNL YANLRPCNFM SEKLLDLSPL
     RSEIVKGTNF TVVRELVGGI YFGTRKEDEG NGEAWDTEKY TVEEVKRITR MAAFLALQSN
     PPLPVWSLDK ANVLASSRLW RKTVTETIEK EFPQLTLNHQ LIDSAAMILI QNPSKMNGVI
     VTSNMFGDII SDEASVIPGS LGLLPSASLS SLPDKNTAFG LYEPCHGSAP DLPPNKVNPI
     ATILSAAMML RLSLNLKEEA DAVEKAVSKV IDNGIVTADL KGASSTTEVG DAVAAEVQKL
     LK
//