ID   LEU3_BURTA              Reviewed;         355 AA.
AC   Q2T7H6;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   04-NOV-2008, entry version 25.
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=BTH_II0674;
OS   Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 /
OS   CIP 106301).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R.,
RA   Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D.,
RA   Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P.,
RA   Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F.,
RA   Roberts K., Hatch B., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) 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 (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.
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DR   EMBL; CP000085; ABC35976.1; -; Genomic_DNA.
DR   RefSeq; YP_438873.1; -.
DR   GeneID; 3845853; -.
DR   GenomeReviews; CP000085_GR; BTH_II0674.
DR   KEGG; bte:BTH_II0674; -.
DR   TIGR; BTH_II0674; -.
DR   HOGENOM; Q2T7H6; -.
DR   BioCyc; BTHA271848:BTH_II0674-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    355       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000250109.
FT   NP_BIND     280    292       NAD (By similarity).
FT   METAL       222    222       Magnesium or manganese (By similarity).
FT   METAL       246    246       Magnesium or manganese (By similarity).
FT   METAL       250    250       Magnesium or manganese (By similarity).
FT   BINDING      90     90       Substrate (By similarity).
FT   BINDING     100    100       Substrate (By similarity).
FT   BINDING     128    128       Substrate (By similarity).
FT   BINDING     222    222       Substrate (By similarity).
FT   SITE        135    135       Important for catalysis (By similarity).
FT   SITE        190    190       Important for catalysis (By similarity).
SQ   SEQUENCE   355 AA;  38242 MW;  CE8C13AF0007C5E4 CRC64;
     MKIAVLPGDG IGPEIVNEAV KVLNALDEKF ELEHAPVGGA GYEASGHPLP DATLALAKEA
     DAILFGAVGD WKYDSLERAL RPEQAILGLR KHLELFANFR PAICYPQLVD ASPLKPELVA
     GLDILIVREL NGDIYFGQPR GVRAAPDGPF AGEREGFDTM RYSEPEVRRI AHVAFQAAQK
     RAKKLLSVDK SNVLETSQFW RDVMIDVSKE YADVELSHMY VDNAAMQLAK APKQFDVIVT
     GNMFGDILSD EASMLTGSIG MLPSASLDKN NKGLYEPSHG SAPDIAGKGI ANPLATILSA
     AMLLRYSLNR AEQADRIERA VKTVLEQGYR TGDIATPGCR QVGTAAMGDA VVAAL
//