ID   LEU3_BUCUD              Reviewed;         363 AA.
AC   Q9EVE1;
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 rudbeckiae.
OG   Plasmid pLeu (pBAp1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=118114;
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; AF200469; AAG31928.1; -; 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    363       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083668.
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;  40543 MW;  52E9BE62DC807AED CRC64;
     MKKKYRIAVL PGDGIGPEVM REAYKILNIL KNHFSLPLET REFNIGGSAI DQEGTALPKK
     TLLGCENSDA ILFGSVGGKK WDDLPINQRP ERASLLPLRK HFNLFANLRP AKLYSELKYL
     SPLRSDIIKN GFDILCIREL TGGLYFGKPT GRLKKNNIEY AFDTEIYYNY EITRIAHLAF
     QLAQTRNFKI CSIDKSNVLN SSVLWREIVK KVSKNYPDVH LSHLYIDNAT MQIIKDPNQF
     DILLCSNLFG DIISDECAII TGSIGMLPSA SLNEKKFGLY EPAGGSAPDI EGKNIANPIA
     QILSVSMLVR YGMNLKTIAD KIDQSVISVL KKGYRTADIS NNNNYLKTNE MGDVIANTLI
     SGE
//