ID   LEU3_BUCAP              Reviewed;         363 AA.
AC   O85064;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 49.
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=BUsg_PL5;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OG   Plasmid pLeu-Sg (pBSg1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=99091706; PubMed=9873079; DOI=10.1007/PL00006447;
RA   Baumann L., Baumann P., Moran N.A., Sandstroem J.P., Thao M.L.;
RT   "Genetic characterization of plasmids containing genes encoding
RT   enzymes of leucine biosynthesis in endosymbionts (Buchnera) of
RT   aphids.";
RL   J. Mol. Evol. 48:77-85(1999).
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; AF041836; AAD12594.1; -; Genomic_DNA.
DR   RefSeq; NP_047181.1; -.
DR   HSSP; P37412; 1CNZ.
DR   GeneID; 2648309; -.
DR   GenomeReviews; AF041836_GR; BUsg_PL5.
DR   HOGENOM; O85064; -.
DR   OMA; O85064; EAFDTMR.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0051287; F:NAD or NADH binding; IEA:InterPro.
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; 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   Complete proteome; Cytoplasm; Leucine biosynthesis; Magnesium;
KW   Manganese; Metal-binding; NAD; Oxidoreductase; Plasmid.
FT   CHAIN         1    363       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083661.
FT   NP_BIND      78     91       NAD (By similarity).
FT   NP_BIND     285    297       NAD (By similarity).
FT   METAL       227    227       Magnesium or manganese (By similarity).
FT   METAL       251    251       Magnesium or manganese (By similarity).
FT   METAL       255    255       Magnesium or manganese (By similarity).
FT   BINDING      99     99       Substrate (By similarity).
FT   BINDING     109    109       Substrate (By similarity).
FT   BINDING     138    138       Substrate (By similarity).
FT   BINDING     227    227       Substrate (By similarity).
FT   SITE        145    145       Important for catalysis (By similarity).
FT   SITE        195    195       Important for catalysis (By similarity).
SQ   SEQUENCE   363 AA;  40918 MW;  1B70FDAEF9EC7D60 CRC64;
     MKKKFRIAVL PGDGIGPEVM REAYKILNIL ERKFFLKLEL REFDIGGIAI DREGIALPEK
     TLRGCENSDA ILFGSVGGKK WDYLPIESRP ERASLLPLRK HFNLFSNLRP AKLRVDLKNL
     SPLRSDIVRD GFDILCIREL TGGIYFGKPK GRFKNKNGEY AFDTEIYYDF EIERIANLAF
     ELASSRRCKV CSIDKANVLE SSVLWREIVK KVSKNYPDVH LSHLYIDNAC MQIIKNPTQF
     DILLCSNIFG DIISDECAMI TGSIGMLPSA SLNNQKFGLY EPAGGSAPDI EGKNIANPIA
     QILSLSMLIR YSMNLNEIAD KIDLSVHYAL KEGYRTLDIS DGKNYIKTNE MGDIIAEFLD
     NGK
//