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Database: UniProt
Entry: Q5WEN4
LinkDB: Q5WEN4
Original site: Q5WEN4 
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   26-NOV-2014, entry version 75.
DE   RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01033};
DE            EC=1.1.1.85 {ECO:0000255|HAMAP-Rule:MF_01033};
DE   AltName: Full=3-IPM-DH {ECO:0000255|HAMAP-Rule:MF_01033};
DE   AltName: Full=Beta-IPM dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01033};
DE            Short=IMDH {ECO:0000255|HAMAP-Rule:MF_01033};
GN   Name=leuB {ECO:0000255|HAMAP-Rule:MF_01033};
GN   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. {ECO:0000255|HAMAP-Rule:MF_01033}.
CC   -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-
CC       2-oxopentanoate + CO(2) + NADH. {ECO:0000255|HAMAP-Rule:MF_01033}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01033};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01033};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01033};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 3/4.
CC       {ECO:0000255|HAMAP-Rule:MF_01033}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01033}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01033}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. LeuB type 1 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01033}.
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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; CEANSIL; -.
DR   OrthoDB; EOG65N1BN; -.
DR   BioCyc; BCLA66692:GHMP-2720-MONOMER; -.
DR   UniPathway; UPA00048; UER00072.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-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:UniProtKB-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; Reference proteome.
FT   CHAIN         1    364       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083637.
FT   NP_BIND      76     89       NAD. {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   NP_BIND     281    293       NAD. {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   METAL       223    223       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   METAL       247    247       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   METAL       251    251       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   BINDING      96     96       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01033}.
FT   BINDING     106    106       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01033}.
FT   BINDING     134    134       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01033}.
FT   BINDING     223    223       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01033}.
FT   SITE        141    141       Important for catalysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   SITE        191    191       Important for catalysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
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
//
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