ID   LEU3_BACFR              Reviewed;         353 AA.
AC   P54354;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   04-NOV-2008, entry version 58.
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=BF3444;
OS   Bacteroides fragilis.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YCH46;
RX   MEDLINE=96025424; PubMed=8569539;
RA   Sarker M.R., Akimoto S., Ugai H., Kuwahara T., Ohnishi Y.;
RT   "Nucleotide sequence of the gene encoding beta-isopropylmalate
RT   dehydrogenase (leuB) from Bacteroides fragilis.";
RL   Microbiol. Immunol. 39:525-529(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA
RT   inversions regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. LeuB type 1 subfamily.
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DR   EMBL; D45169; BAA08117.1; -; Genomic_DNA.
DR   EMBL; AP006841; BAD50187.1; -; Genomic_DNA.
DR   PIR; I40235; I40235.
DR   RefSeq; YP_100721.1; -.
DR   HSSP; P00351; 1DR8.
DR   GeneID; 3084526; -.
DR   GenomeReviews; AP006841_GR; BF3444.
DR   KEGG; bfr:BF3444; -.
DR   HOGENOM; P54354; -.
DR   BioCyc; BFRA295405:BF3444-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
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:0009098; P:leucine biosynthetic process; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01033; -; 1.
DR   InterPro; IPR004429; 3-isopropylmalate_DHase.
DR   InterPro; IPR001804; IsoCit_IM_DHase.
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    353       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083644.
FT   METAL       219    219       Magnesium or manganese (By similarity).
FT   METAL       243    243       Magnesium or manganese (By similarity).
FT   METAL       247    247       Magnesium or manganese (By similarity).
FT   BINDING      97     97       Substrate (By similarity).
FT   BINDING     107    107       Substrate (By similarity).
FT   BINDING     135    135       Substrate (By similarity).
FT   BINDING     219    219       Substrate (By similarity).
FT   SITE        142    142       Important for catalysis (By similarity).
FT   SITE        187    187       Important for catalysis (By similarity).
SQ   SEQUENCE   353 AA;  39098 MW;  355259EA221F4A84 CRC64;
     MDFKIAVLAG DGIGPEISVQ GVEVMSAVCE KFGHKVNYEY AICGADAIDK VGDPFPEETY
     RVCKNADAVL FSAVGDPKFD NDPTAKVRPE QGLLAMRKKL GLFANIRPVQ TFKCLVHKSP
     LRAELVEGAD FLCIRELTGG MYFGEKYQDN DKAYDTNMYT RPEIERILKV GFEYAMKRRK
     HLTVVDKANV LASSRLWRQI AQEMAPQYPE VTTDYMFVDN AAMKMIQEPK FFDVMVTENT
     FGDILTDEGS VISGSMGLLP SASTGESTPV FEPIHGSWPQ AKGLNIANPL AQILSVAMLF
     EYFDCKAEGA LIRKAVDASL DANVRTPEIQ VEGGEKFGTK EVGAWIVDYI RKA
//