ID   LEU3_BACLD              Reviewed;         370 AA.
AC   Q65GI9; Q62RZ7;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   04-NOV-2008, entry version 34.
DE   RecName: Full=3-isopropylmalate dehydrogenase;
DE            EC=1.1.1.85;
DE   AltName: Full=Beta-IPM dehydrogenase;
DE            Short=IMDH;
DE   AltName: Full=3-IPM-DH;
GN   Name=leuB; OrderedLocusNames=BLi02957, BL00612;
OS   Bacillus licheniformis (strain DSM 13 / ATCC 14580).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H.,
RA   Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R.,
RA   Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an
RT   organism with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G.,
RA   Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L.,
RA   Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N.,
RA   Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(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 (By similarity).
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. LeuB type 1 subfamily.
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DR   EMBL; AE017333; AAU41825.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP000002; AAU24463.1; -; Genomic_DNA.
DR   RefSeq; YP_080101.1; -.
DR   RefSeq; YP_092518.1; -.
DR   GeneID; 3028335; -.
DR   GeneID; 3098436; -.
DR   GenomeReviews; CP000002_GR; BL00612.
DR   GenomeReviews; AE017333_GR; BLi02957.
DR   KEGG; bld:BLi02957; -.
DR   KEGG; bli:BL00612; -.
DR   NMPDR; fig|279010.5.peg.3307; -.
DR   HOGENOM; Q65GI9; -.
DR   BioCyc; BLIC279010:BL00612-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:HAMAP.
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:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01033; -; 1.
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   Complete proteome; Cytoplasm; Leucine biosynthesis; Magnesium;
KW   Manganese; Metal-binding; NAD; Oxidoreductase.
FT   CHAIN         1    370       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083640.
FT   NP_BIND      76     89       NAD (By similarity).
FT   NP_BIND     282    294       NAD (By similarity).
FT   METAL       224    224       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      96     96       Substrate (By similarity).
FT   BINDING     106    106       Substrate (By similarity).
FT   BINDING     134    134       Substrate (By similarity).
FT   BINDING     224    224       Substrate (By similarity).
FT   SITE        141    141       Important for catalysis (By similarity).
FT   SITE        192    192       Important for catalysis (By similarity).
SQ   SEQUENCE   370 AA;  39850 MW;  9F23133E6AECED1C CRC64;
     MKKRIALLPG DGIGPEVLDA AVDVLKSVAE HYQHEFEFEY GLIGGAAIDE AGAPLPEETV
     AACKAADAIL LGAVGGPKWD QNPSELRPEK GLLAIRKQLD LFANLRPVKV FESLAGASPL
     KTEYIEGVDF VIVRELTGGL YFGKPSEQYV NQNGEEEAVD TLFYKKSEME RVIREAFQMA
     QSRKGKVTSV DKANVLESSK LWRKTAEEVA KEFPDVKLEH MLVDNAAMQL IYAPGQFDII
     VTENMFGDIL SDEASMLTGS LGMLPSASLS SSGLHLYEPV HGSAPDIAGQ NIANPLAAIL
     SAAMMLRTSF GLEAEAQAVE HAVDQVLRAG KRTKDLAKGS EHCTTQSITG EVKAALADDN
     AISNIMTAYV
//