ID LEU3_BACSK Reviewed; 364 AA.
AC Q5WEN4;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 29-MAY-2013, entry version 68.
DE RecName: Full=3-isopropylmalate dehydrogenase;
DE EC=1.1.1.85;
DE AltName: Full=3-IPM-DH;
DE AltName: Full=Beta-IPM dehydrogenase;
DE Short=IMDH;
GN Name=leuB; OrderedLocusNames=ABC2641;
OS Bacillus clausii (strain KSM-K16).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=66692;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSM-K16;
RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA Kawai S., Ito S., Horikoshi K.;
RT "The complete genome sequence of the alkaliphilic Bacillus clausii
RT KSM-K16.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
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; AP006627; BAD65176.1; -; Genomic_DNA.
DR RefSeq; YP_176137.1; NC_006582.1.
DR ProteinModelPortal; Q5WEN4; -.
DR SMR; Q5WEN4; 1-356.
DR STRING; 66692.ABC2641; -.
DR EnsemblBacteria; BAD65176; BAD65176; ABC2641.
DR GeneID; 3204057; -.
DR KEGG; bcl:ABC2641; -.
DR PATRIC; 18924928; VBIBacCla58185_2816.
DR eggNOG; COG0473; -.
DR HOGENOM; HOG000021112; -.
DR KO; K00052; -.
DR OMA; STIAGCE; -.
DR ProtClustDB; PRK00772; -.
DR BioCyc; BCLA66692:GHMP-2720-MONOMER; -.
DR UniPathway; UPA00048; UER00072.
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:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.40.718.10; -; 1.
DR HAMAP; MF_01033; LeuB_type1; 1; -.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR004429; Isopropylmalate_DH.
DR PANTHER; PTHR11835; PTHR11835; 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 1 364 3-isopropylmalate dehydrogenase.
FT /FTId=PRO_0000083637.
FT NP_BIND 76 89 NAD (By similarity).
FT NP_BIND 281 293 NAD (By similarity).
FT METAL 223 223 Magnesium or manganese (By similarity).
FT METAL 247 247 Magnesium or manganese (By similarity).
FT METAL 251 251 Magnesium or manganese (By similarity).
FT BINDING 96 96 Substrate (By similarity).
FT BINDING 106 106 Substrate (By similarity).
FT BINDING 134 134 Substrate (By similarity).
FT BINDING 223 223 Substrate (By similarity).
FT SITE 141 141 Important for catalysis (By similarity).
FT SITE 191 191 Important for catalysis (By similarity).
SQ SEQUENCE 364 AA; 39332 MW; 232EC25567427128 CRC64;
MEKQILLLPG DGIGPEIIAE TKRVLEEIAR LYHHTFQFVE GRIGGDAIDA TGSPLPEETL
DLAKGSDAIL LGAVGGPKWD GNAPEKRPEK GLLQIRKALG LYANLRPVRV LKPLMGASTL
KEEVLADVDL LIVRELTGGL YFGEPRERRQ INGEDGAVDT LLYTRGEIER IVHQAFQFAR
TRKKRVVSVD KANVLESSRL WREIADEVAR EYPDVTLSHM LVDNAAMQLI RDPRQFDVIV
TENLFGDILS DEASMITGSL GLLPSASMNT SKVGLFEPVH GSAPDIAGTG AANPLATILS
AAMMLQYSFG LADEAKAIEV AVDRVLAQGV RTKDIAKASE NAVSTTAITN AVMEALALKS
ASSR
//
