ID   LEU3_CAMJE              Reviewed;         358 AA.
AC   Q9PLW0; Q0P7R3;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   04-NOV-2008, entry version 46.
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=Cj1718c;
OS   Campylobacter jejuni.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 11168 / Serotype O:2;
RX   MEDLINE=20150912; PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W.,
RA   Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M.,
RA   Whitehead S., Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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; AL111168; CAL35812.1; -; Genomic_DNA.
DR   PIR; B81270; B81270.
DR   HSSP; P37412; 1CNZ.
DR   IntAct; Q9PLW0; -.
DR   GenomeReviews; AL111168_GR; Cj1718c.
DR   KEGG; cje:Cj1718c; -.
DR   BioCyc; CJEJ192222:CJ1718C-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    358       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083675.
FT   NP_BIND      77     90       NAD (By similarity).
FT   NP_BIND     279    291       NAD (By similarity).
FT   METAL       221    221       Magnesium or manganese (By similarity).
FT   METAL       245    245       Magnesium or manganese (By similarity).
FT   METAL       249    249       Magnesium or manganese (By similarity).
FT   BINDING      98     98       Substrate (By similarity).
FT   BINDING     108    108       Substrate (By similarity).
FT   BINDING     137    137       Substrate (By similarity).
FT   BINDING     221    221       Substrate (By similarity).
FT   SITE        144    144       Important for catalysis (By similarity).
FT   SITE        189    189       Important for catalysis (By similarity).
SQ   SEQUENCE   358 AA;  39368 MW;  26B811645E7FFA83 CRC64;
     MKTYKVAVLA GDGIGPLVMK EALKILTFIA QKYNFSFEFN EAKIGGASID AYGVALSDET
     LKLCEQSDAI LFGSVGGPKW DNLPIDQRPE RASLLPLRKH FNLFANLRPC KIYESLTHAS
     PLKNEIIQKG VDILCVRELT GGIYFGKQDL GKESAYDTEI YTKKEIERIA RIAFESARIR
     KKKVHLIDKA NVLASSILWR EVVANVAKDY QDINLEYMYV DNAAMQIVKN PSIFDVMLCS
     NLFGDILSDE LAAINGSLGL LSSASLNDKG FGLYEPAGGS APDIAHLNIA NPIAQILSAA
     LMLKYSFKEE QAAQDIENAI SLALAQGKMT KDLNAKSYLN TDEMGDCILE ILKENDNG
//