ID   LEU3_CLOAB              Reviewed;         357 AA.
AC   Q97EE2;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   16-JUN-2009, entry version 51.
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; OrderedLocusNames=CA_C3171;
OS   Clostridium acetobutylicum.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   MEDLINE=21359325; PubMed=11466286;
RX   DOI=10.1128/JB.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q.,
RA   Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I.,
RA   Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P.,
RA   Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE001437; AAK81108.1; -; Genomic_DNA.
DR   PIR; A97290; A97290.
DR   RefSeq; NP_349768.1; -.
DR   HSSP; Q56268; 1A05.
DR   GeneID; 1119353; -.
DR   GenomeReviews; AE001437_GR; CA_C3171.
DR   KEGG; cac:CAC3171; -.
DR   NMPDR; fig|272562.1.peg.3297; -.
DR   HOGENOM; Q97EE2; -.
DR   OMA; Q97EE2; EAFDTMR.
DR   BioCyc; CACE272562:CAC3171-MON; -.
DR   BRENDA; 1.1.1.85; 2866.
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   Complete proteome; Cytoplasm; Leucine biosynthesis; Magnesium;
KW   Manganese; Metal-binding; NAD; Oxidoreductase.
FT   CHAIN         1    357       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083680.
FT   NP_BIND      77     90       NAD (By similarity).
FT   NP_BIND     282    294       NAD (By similarity).
FT   METAL       224    224       Magnesium or manganese (By similarity).
FT   METAL       248    248       Magnesium or manganese (By similarity).
FT   METAL       252    252       Magnesium or manganese (By similarity).
FT   BINDING      97     97       Substrate (By similarity).
FT   BINDING     107    107       Substrate (By similarity).
FT   BINDING     136    136       Substrate (By similarity).
FT   BINDING     224    224       Substrate (By similarity).
FT   SITE        143    143       Important for catalysis (By similarity).
FT   SITE        192    192       Important for catalysis (By similarity).
SQ   SEQUENCE   357 AA;  38980 MW;  E24DF0A2BD2EBC2C CRC64;
     MKEYKVAVIP GDGIGVEIVG EALKVLEKVG AKYDTKFNFT EVKAGGCAID EFGVPLPNET
     LEICKNSDAV LLGAVGGPKW DTLPGEKRPE KALMGLRGGL GLYANLRPAK VYDILKSASP
     LKEEIINKGV DLLVVRELTG GIYFGERGRD IQNGINSAYD TERYNVEEIK RIAHVAFKAA
     LKRNKKVTSV DKANILESSR LWRETVTEVA KEYPEVELNY LYVDNAAMQL VREPSQFDVI
     VTSNIFGDIL TDEASMVTGS IGMLPSASLR NDTFGMYEPI HGSAPDIAGQ DLANPLAQIL
     SVAMMLEYSF NMTEAARDVE DAVEKVLNSG YRTGDIYTEG SKKVGTKEMG KLVLAEL
//