ID   LEU32_BRAJA             Reviewed;         370 AA.
AC   Q89X19;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   04-NOV-2008, entry version 38.
DE   RecName: Full=3-isopropylmalate dehydrogenase 2;
DE            EC=1.1.1.85;
DE   AltName: Full=Beta-IPM dehydrogenase 2;
DE            Short=IMDH 2;
DE   AltName: Full=3-IPM-DH 2;
GN   Name=leuB2; OrderedLocusNames=bll0504;
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.
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; BA000040; BAC45768.1; -; Genomic_DNA.
DR   RefSeq; NP_767143.1; -.
DR   HSSP; Q56268; 1A05.
DR   GeneID; 1049819; -.
DR   GenomeReviews; BA000040_GR; bll0504.
DR   KEGG; bja:bll0504; -.
DR   NMPDR; fig|224911.1.peg.503; -.
DR   HOGENOM; Q89X19; -.
DR   BioCyc; BJAP224911:BLL0504-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 2.
FT                                /FTId=PRO_0000083652.
FT   NP_BIND      77     90       NAD (By similarity).
FT   NP_BIND     290    302       NAD (By similarity).
FT   METAL       226    226       Magnesium or manganese (By similarity).
FT   METAL       250    250       Magnesium or manganese (By similarity).
FT   METAL       254    254       Magnesium or manganese (By similarity).
FT   BINDING      97     97       Substrate (By similarity).
FT   BINDING     107    107       Substrate (By similarity).
FT   BINDING     135    135       Substrate (By similarity).
FT   BINDING     226    226       Substrate (By similarity).
FT   SITE        142    142       Important for catalysis (By similarity).
FT   SITE        193    193       Important for catalysis (By similarity).
SQ   SEQUENCE   370 AA;  39707 MW;  54FB249F9F1578AD CRC64;
     MATHKLLLLP GDGIGPEVMG EVKRLIDWLN SAGIAKFETD TGLVGGSAYD AHKVSISEGD
     MAKALAADAI IFGAVGGPKW DAVPYEVRPE AGLLRLRKDL GLFANLRPAV CYPALADASS
     LKREAVEGLD IMIVRELTGG VYFGEPKTIT DLGNGQKRAI DTQVYDTYEI ERIARVAFDL
     AKKRKNKVTS MEKRNVMKSG VLWNEVVTQV HKREYPDVTL EHQLADSGGM MLVKWPKQFD
     VIVTDNLFGD MLSDIAAMLT GSLGMLPSAS LGEVDVKSKK RKALYEPVHG SAPDIAGKGL
     ANPIAMISSF GMALRYSFDM GALADKVDAA IAAVLASGLR TADIKSEGTT AASTTQMGEA
     ILKELQKLHA
//