ID   LEU3_BUCPS              Reviewed;         363 AA.
AC   P59027;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 41.
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. Pemphigus spyrothecae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98799;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=21972315; PubMed=11976137;
RX   DOI=10.1128/AEM.68.5.2572-2575.2002;
RA   Sabater-Munoz B., Gomez-Valero L., van Ham R.C.H.J., Silva F.J.,
RA   Latorre A.;
RT   "Molecular characterization of the leucine cluster in Buchnera sp.
RT   strain PSY, a primary endosymbiont of the aphid Pemphigus
RT   spyrothecae.";
RL   Appl. Environ. Microbiol. 68:2572-2575(2002).
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; AJ426489; CAD20138.1; -; Genomic_DNA.
DR   HSSP; P30125; 1CM7.
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.
FT   CHAIN         1    363       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083659.
FT   NP_BIND      77     90       NAD (By similarity).
FT   NP_BIND     284    296       NAD (By similarity).
FT   METAL       226    226       Magnesium or manganese (By similarity).
FT   METAL       250    250       Magnesium or manganese (By similarity).
FT   METAL       254    254       Magnesium or manganese (By similarity).
FT   BINDING      98     98       Substrate (By similarity).
FT   BINDING     108    108       Substrate (By similarity).
FT   BINDING     137    137       Substrate (By similarity).
FT   BINDING     226    226       Substrate (By similarity).
FT   SITE        144    144       Important for catalysis (By similarity).
FT   SITE        194    194       Important for catalysis (By similarity).
SQ   SEQUENCE   363 AA;  40550 MW;  760AAA94425D6632 CRC64;
     MTKIYNLAIL PGDGIGPELL QKDLNFKVLK EQYKLKINTT EYDIGGIAID KYGKALPKET
     LDGCKESDSI LFGSVGGPKW QHLPPDQQPE RAALLPIRKY FNLFSNLRPA KLYSTLNHLS
     PLRRDISEKG FDILCVRELT GGIYFGKPKG YIKNIIDKKA FDTEIYYASE IKRIAHIGFK
     LAQNRKYKIT SVDKANVLES SVLWRETVNT ISKEYPDVKL SHLYIDHAAM QIIKNPDKFD
     VILTSNLFGD ILSDECAMIT GSIGMLPSAS LNDSNFGLYE PAGGSAPDIA GKNIANPIAQ
     ILSIAMLVRY TMKLPMISDH IESAVIDTLK KGYRTLDIAN DKEKYVSTND IGDIISDILK
     KRI
//