ID   LEU32_BORBR             Reviewed;         358 AA.
AC   Q7WKH4;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   16-JUN-2009, entry version 41.
DE   RecName: Full=3-isopropylmalate dehydrogenase 2;
DE            EC=1.1.1.85;
DE   AltName: Full=Beta-IPM dehydrogenase 2;
DE            Short=IMDH 2;
DE   AltName: Full=3-IPM-DH 2;
GN   Name=leuB2; OrderedLocusNames=BB2132;
OS   Bordetella bronchiseptica (Alcaligenes bronchisepticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RB50 / ATCC BAA-588 / NCTC 13252;
RX   MEDLINE=22827954; PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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; BX640443; CAE32628.1; -; Genomic_DNA.
DR   RefSeq; NP_888675.1; -.
DR   GeneID; 2660922; -.
DR   GenomeReviews; BX470250_GR; BB2132.
DR   KEGG; bbr:BB2132; -.
DR   HOGENOM; Q7WKH4; -.
DR   OMA; Q7WKH4; EAFDTMR.
DR   BioCyc; BBRO257310:BB2132-MON; -.
DR   BRENDA; 1.1.1.85; 413.
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    358       3-isopropylmalate dehydrogenase 2.
FT                                /FTId=PRO_0000083649.
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      92     92       Substrate (By similarity).
FT   BINDING     102    102       Substrate (By similarity).
FT   BINDING     130    130       Substrate (By similarity).
FT   BINDING     224    224       Substrate (By similarity).
FT   SITE        137    137       Important for catalysis (By similarity).
FT   SITE        192    192       Important for catalysis (By similarity).
SQ   SEQUENCE   358 AA;  38541 MW;  719D3DDAF951DAEC CRC64;
     MTHQIAVLPG DGIGPEIVEQ AERVLKALDL PLELRQAPVG GAAFDQFEHP LPPATLELAQ
     GSHAVLFGAV GDWKYDTLPR EFRPEQAILG LRKALGLFAN LRPAILYPEL ASASSLKPEI
     VSGLDILIIR ELTGDIYFGT PRGVRTAADG AFAGEREGYD TMRYAESEVR RIARIGFESA
     RKRNKKLCSV DKANVLETSQ FWRDLVIEVS RDYPDVELSH MYVDNAAMQL VRNPRQFDVI
     VTGNLFGDIL SDEAAMLTGS IGMLPSASLN AAGQGLYEPS HGSAPDIAGQ GIANPLATIL
     SAAMLLRYSL NLAPQADRVE AAVRKVLADG LRTADIHEAG TTKVSTSQMG DAVLKALG
//