ID   LEU31_BRAJA             Reviewed;         379 AA.
AC   Q89XA0;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   04-NOV-2008, entry version 38.
DE   RecName: Full=3-isopropylmalate dehydrogenase 1;
DE            EC=1.1.1.85;
DE   AltName: Full=Beta-IPM dehydrogenase 1;
DE            Short=IMDH 1;
DE   AltName: Full=3-IPM-DH 1;
GN   Name=leuB1; OrderedLocusNames=bll0414;
OS   Bradyrhizobium japonicum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USDA 110;
RX   MEDLINE=22484998; PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T.,
RA   Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K.,
RA   Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M.,
RA   Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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 (By similarity).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BA000040; BAC45679.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_767054.1; -.
DR   HSSP; Q56268; 1A05.
DR   GeneID; 1054690; -.
DR   GenomeReviews; BA000040_GR; bll0414.
DR   KEGG; bja:bll0414; -.
DR   NMPDR; fig|224911.1.peg.414; -.
DR   HOGENOM; Q89XA0; -.
DR   BioCyc; BJAP224911:BLL0414-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    379       3-isopropylmalate dehydrogenase 1.
FT                                /FTId=PRO_0000250104.
FT   NP_BIND     293    305       NAD (By similarity).
FT   METAL       230    230       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     101    101       Substrate (By similarity).
FT   BINDING     111    111       Substrate (By similarity).
FT   BINDING     139    139       Substrate (By similarity).
FT   BINDING     230    230       Substrate (By similarity).
FT   SITE        146    146       Important for catalysis (By similarity).
FT   SITE        197    197       Important for catalysis (By similarity).
SQ   SEQUENCE   379 AA;  40723 MW;  0B418C546FC8D01C CRC64;
     MNTLSNTITV AVVGGEGIGP EVTDQSHRIL KWFSDRRGAP VILREAQYGL IPYLATGKVL
     PDDTVEAMEE ADAILWGATG GPETTEVPPA ARKAGSLLSL RSKYDLYANL RPIVANPALA
     DSAPLKAAVL KDVDFIIIRE LTSGIYFGEP RGIETLPDGQ RRGFNTQQYT TSQIRRVART
     AFELARTRKG RVCSVDKANV LETSVLWREE VTALHEAEFS DVELTHLYVD NAAMQIVRAP
     SQFDVMVTCN IFGDILSDCA AMASGSLGML PSVSLGPPDR LGRRKALYEP VHGSAPDIAG
     KGIANPLGSI LSVAMMLRIT LHRPEDAALL EKAVDTALAA GARTADIAEP GAKRLSTQEM
     GDAVLNALDK VVGKEREHA
//