ID   LEU3_CEPAC              Reviewed;         380 AA.
AC   Q12545;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 51.
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   Cephalosporium acremonium (Acremonium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales;
OC   mitosporic Hypocreales; Acremonium.
OX   NCBI_TaxID=5044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M8650;
RA   Kimura H., Matumura S., Suzuki M., Sumino Y.;
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
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; D50665; BAA09319.1; -; Genomic_DNA.
DR   HSSP; P12010; 2AYQ.
DR   BRENDA; 1.1.1.85; 66776.
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   Cytoplasm; Leucine biosynthesis; Magnesium; Manganese; Metal-binding;
KW   NAD; Oxidoreductase.
FT   CHAIN         1    380       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083607.
FT   NP_BIND      79     90       NAD (By similarity).
FT   NP_BIND     294    306       NAD (By similarity).
FT   METAL       229    229       Magnesium or manganese (By similarity).
FT   METAL       254    254       Magnesium or manganese (By similarity).
FT   METAL       258    258       Magnesium or manganese (By similarity).
FT   BINDING      97     97       Substrate (By similarity).
FT   BINDING     107    107       Substrate (By similarity).
FT   BINDING     136    136       Substrate (By similarity).
FT   BINDING     229    229       Substrate (By similarity).
FT   SITE        143    143       Important for catalysis (By similarity).
FT   SITE        196    196       Important for catalysis (By similarity).
SQ   SEQUENCE   380 AA;  40637 MW;  0F99ACD5251CCB43 CRC64;
     MTTTYKILVL PGDHIGPEIM AEAIKVLTTI ETHRPNLHFN LTTDLVGGTS IDTHGVPITQ
     SVLDAAKASD AVLFGSIGGP EWAGVHPTPE SGLLQLRQHL DAFANLRPCE FLVPSLVGAS
     PIREHVVKGT RFIVVRENCG GAYFGEKKEE EDVASDLWVY TRPEIERLAR VSAAVARIMG
     RSEDDNQAAT VWSADKANVL ASGRLWRRIT SDIFAKEFPD ITLQHQLADS MAMLMVRDPR
     RFNGVIHTDN TFGDILSDIS GAITGTLGLM PSASLCGVPG EGHRSNGIYE PVHGSAPDIS
     GKGLANPVAQ ILSVAMMLRY SMGLEKEATA VERAVVKVLD AKSEGGLEIR TGDLGGRATC
     SQVGDAVCEV LGPLLQGKKA
//