ID   LEU3_BUCML              Reviewed;         365 AA.
AC   Q9EVG3;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   04-NOV-2008, entry version 40.
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;
OS   Buchnera aphidicola subsp. Macrosiphoniella ludovicianae.
OG   Plasmid pLeu (pBAp1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=118105;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=20576185; PubMed=11133977; DOI=10.1128/JB.183.2.785-790.2001;
RA   Wernegreen J.J., Moran N.A.;
RT   "Vertical transmission of biosynthetic plasmids in aphid endosymbionts
RT   (Buchnera).";
RL   J. Bacteriol. 183:785-790(2001).
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; AF197456; AAG31402.1; -; Genomic_DNA.
DR   HSSP; P37412; 1CNZ.
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   Cytoplasm; Leucine biosynthesis; Magnesium; Manganese; Metal-binding;
KW   NAD; Oxidoreductase; Plasmid.
FT   CHAIN         1    365       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083658.
FT   NP_BIND      78     91       NAD (By similarity).
FT   NP_BIND     286    298       NAD (By similarity).
FT   METAL       228    228       Magnesium or manganese (By similarity).
FT   METAL       252    252       Magnesium or manganese (By similarity).
FT   METAL       256    256       Magnesium or manganese (By similarity).
FT   BINDING      99     99       Substrate (By similarity).
FT   BINDING     109    109       Substrate (By similarity).
FT   BINDING     139    139       Substrate (By similarity).
FT   BINDING     228    228       Substrate (By similarity).
FT   SITE        146    146       Important for catalysis (By similarity).
FT   SITE        196    196       Important for catalysis (By similarity).
SQ   SEQUENCE   365 AA;  40966 MW;  213AEB0F71DF960C CRC64;
     MKKQYRIAVL PGDGIGPEVM KEAYKILKIL QNYFSLHIEI KEFNIGGIAL DKEGVALPKD
     TLLGCENSDA ILFGSVGGKK WNNLPIEKRP ERASLLPLRK HFNLFYNLRP AKLYSELRFL
     SPLRSKTXIK NGFDILCIRE LTGGIYFGEP RGRLKKNNIE YAFDTEVYYD YEINRIAHVA
     FQLARTRKNK VCSIDKANVL NSSLLWREIV TKVSKNYPDV HLSHLYIDNA TMQIIQNPNQ
     FDILLCSNLF GDILSDECAI ITGSIGMLPS ASLNEKNFGL YEPAGGSAPD IAGKNIANPI
     AQILSLSMLV RYGMNLKKIA NKIDQSVISV LKKGYRTFDI SDDNNXFLKT NEMGDVIADA
     LINGE
//