ID   LEU3_BUCTS              Reviewed;         364 AA.
AC   O31292;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 50.
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. Thelaxes suberi.
OG   Plasmid pBTs1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=97386415; PubMed=9244264;
RA   van Ham R.C.H.J., Moya A., Latorre A.;
RT   "Putative evolutionary origin of plasmids carrying the genes involved
RT   in leucine biosynthesis in Buchnera aphidicola (endosymbiont of
RT   aphids).";
RL   J. Bacteriol. 179:4768-4777(1997).
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; Y11966; CAA72702.1; -; Genomic_DNA.
DR   HSSP; P37412; 1CNZ.
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    364       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083662.
FT   NP_BIND      79     92       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     100    100       Substrate (By similarity).
FT   BINDING     110    110       Substrate (By similarity).
FT   BINDING     139    139       Substrate (By similarity).
FT   BINDING     227    227       Substrate (By similarity).
FT   SITE        146    146       Important for catalysis (By similarity).
FT   SITE        195    195       Important for catalysis (By similarity).
SQ   SEQUENCE   364 AA;  40353 MW;  D3EBFFE1DC07ACF2 CRC64;
     MTKKLYKIAV LPGDGIGPEI IQEAYKIIDV LQKKFSFNVK MHEYDIGGIS IDKHGTALTQ
     ETIEGCENSD AILFGSVGGS KWDHLPEIEK PEKAGLLKLR KHFNLFANIR PCKLSQHLLD
     ISPLKNSIIK KGIDLICIRE LTGGIYFGKS NKITNIDDPY AFDTEIYFRS EIKRIAKIAF
     QIAQSRKKKI VSIDKANVLK SSILWRDTVN KMAYKFPNVK LEHMYIDNAT MELIKNPSSF
     DVILCSNLFG DIISDECAAI IGSIGLLPSA SLNKSGFGLY EPAGGSAPNI AGKTIANPIA
     QILSLSMLLK YSLHLPFLSS CIDEAVHEAL VKKYMTMDIS KNPQNFLKTN EIGDKISDLL
     AKKA
//