ID   LEU3_BUCDN              Reviewed;         363 AA.
AC   O85071;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 46.
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. Diuraphis noxia.
OG   Plasmid pLeu-Dn (pBDn1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=118101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [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; AF041837; AAD12601.1; -; Genomic_DNA.
DR   RefSeq; NP_047188.1; -.
DR   HSSP; P37412; 1CNZ.
DR   GeneID; 1246503; -.
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   Cytoplasm; Leucine biosynthesis; Magnesium; Manganese; Metal-binding;
KW   NAD; Oxidoreductase; Plasmid.
FT   CHAIN         1    363       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083657.
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;  41056 MW;  C4B5F8B3E4F00735 CRC64;
     MHKQYHIAVL PGDGIGPEVM QEAYKILQVL REHFSLFIKT KEFDIGGIAI DNHGIALPKK
     TLIGCENSDA ILLGSIGGKK WDTLPINERP ERASLLPLRK HFNFFCNLRP SNLYKELNFL
     SPLRNDIVKH GFDILCVREL TGGIYFGKPR GRVTKKKLMY AFDTEIYYKF EIVRIAHLAF
     KLARSRKHKL CSIDKANVLE SSILWREVVE EVSKEYPDVI LSHLYIDNVC MQIIKDPNQF
     DVLLCSNLFG DIISDECAMI TGSIGMLPSA SLNEKNFGLY EPAGGSAPDI QGKNIANPIA
     QILSLSMLIR YSMNLNKIAN KIDNAVINVL KKGYKTMDIS KDQNYLKTNE MGDVIADFLK
     RDK
//