ID   LEU3_BIFLO              Reviewed;         343 AA.
AC   Q8G500;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 34.
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=BL1218;
OS   Bifidobacterium longum.
OC   Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=216816;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   MEDLINE=22294977; PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B.,
RA   Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M.,
RA   Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation
RT   to the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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 2 subfamily.
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DR   EMBL; AE014295; AAN25025.1; -; Genomic_DNA.
DR   RefSeq; NP_696389.1; -.
DR   HSSP; P61495; 1IPD.
DR   GeneID; 1022733; -.
DR   GenomeReviews; AE014295_GR; BL1218.
DR   KEGG; blo:BL1218; -.
DR   HOGENOM; Q8G500; -.
DR   OMA; Q8G500; ATRGNER.
DR   BioCyc; BLON206672:BL1218-MON; -.
DR   BRENDA; 1.1.1.85; 39917.
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_01035; -; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR   Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1.
DR   PANTHER; PTHR11835; IDH_IMDH_dimeric; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   PROSITE; PS00470; IDH_IMDH; FALSE_NEG.
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    343       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083794.
FT   NP_BIND     278    290       NAD (By similarity).
FT   METAL       218    218       Magnesium or manganese (By similarity).
FT   METAL       242    242       Magnesium or manganese (By similarity).
FT   METAL       246    246       Magnesium or manganese (By similarity).
FT   BINDING      94     94       Substrate (By similarity).
FT   BINDING     104    104       Substrate (By similarity).
FT   BINDING     128    128       Substrate (By similarity).
FT   BINDING     218    218       Substrate (By similarity).
FT   SITE        135    135       Important for catalysis (By similarity).
FT   SITE        185    185       Important for catalysis (By similarity).
SQ   SEQUENCE   343 AA;  37246 MW;  143417C91B926D30 CRC64;
     MAKTYKIAVI PGDGIGKEVT PWAQKALEKA AEGVADFEYE NFDLGAERYL RDGAILPEDE
     EERIKANDAI LLGAVGDPRI KAGILERGLL LKLRFDLDQY VNLRPSKLYK GVTSPLANPG
     DIDFVVVREG TEGLYCGAGG AVRRNTPQEV ATEVSINTAY GVERVVRYAF KLAMKRKKHV
     TLVHKKNVLV NAGDMWQRIV DKVGEEYPEV THDYQHIDAA TIFLVSDPSR FDVILTDNLF
     GDILTDEAGS VVGGVGYSAS GCINASDEFP SMFEPIHGSA PDIAGQNKAN PTAAILSAAM
     LLEHLGFDDA AKKIHTAVEA DIEELGSTVR STDQVGKDIL ARM
//