ID   LEU3_BUCUO              Reviewed;         364 AA.
AC   Q9EVI1;
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. Uroleucon obscurum.
OG   Plasmid pLeu (pBAp1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=118119;
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; AF197450; AAG31384.1; -; 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    364       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083667.
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     138    138       Substrate (By similarity).
FT   BINDING     228    228       Substrate (By similarity).
FT   SITE        145    145       Important for catalysis (By similarity).
FT   SITE        196    196       Important for catalysis (By similarity).
SQ   SEQUENCE   364 AA;  40604 MW;  261B0E2F34AD57EE CRC64;
     MKTQYRIAVL PGDGIGPEVM REAYKILKIL KNNFLLSFEI EEFNVGGIAI DQEGLALPKK
     TLLGCEKSDA ILFGSVGGKK WDNFPIEERP ERAALLPLRK HFNLFANLRP AKIYSELKHL
     SPLRSNIVRD GFDILCIREL TGGIYFGQPS GRRLEKNNIE YAFDTEIYYD YEINRIAHLA
     FQLAQSRSHK VCSIDKSNVL NSSILWKEIV QKVSKNYPDV DLSHLYIDNA IMQIIKNPNQ
     FDVLLCPNLF GDIISDECAI ITGSIGMLPS ASLNEKKFGL YEPAGGSAPD IAGKNIANPI
     AQILSLSMLV RYGMNLKDIA DKIDKSVLSV LKKGYRTADI SNNNNYLKTN EMGDVIANAL
     ISGE
//