ID   LEU3_AQUAE              Reviewed;         364 AA.
AC   O66607;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 62.
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=aq_244;
OS   Aquifex aeolicus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=63363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC06564.1; -; Genomic_DNA.
DR   PIR; C70322; C70322.
DR   RefSeq; NP_213167.1; -.
DR   HSSP; P00351; 1DPZ.
DR   GeneID; 1192841; -.
DR   GenomeReviews; AE000657_GR; aq_244.
DR   KEGG; aae:aq_244; -.
DR   NMPDR; fig|224324.1.peg.182; -.
DR   HOGENOM; O66607; -.
DR   OMA; O66607; EAFDTMR.
DR   BioCyc; AAEO224324:AQ_244-MON; -.
DR   BRENDA; 1.1.1.85; 189781.
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    364       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083629.
FT   NP_BIND      77     90       NAD (By similarity).
FT   NP_BIND     281    293       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      97     97       Substrate (By similarity).
FT   BINDING     107    107       Substrate (By similarity).
FT   BINDING     135    135       Substrate (By similarity).
FT   BINDING     224    224       Substrate (By similarity).
FT   SITE        142    142       Important for catalysis (By similarity).
FT   SITE        192    192       Important for catalysis (By similarity).
SQ   SEQUENCE   364 AA;  40714 MW;  56B528C760712FAC CRC64;
     MKKYKIAVLK GDGIGPEIVE QALRVLDKIG EIYGVEFEYR EGLIGGEAID KTGDPLPEET
     LKICKESDAI LLGAVGGPKW DNLPTDKRPE KGLLRIRKEL DLYANLRPAK VWDALISSSP
     LKEEVVKGTD MIVIRELTSG IYYGEPRGIF EENGKRYAIN TMKYTEDEIR RIVRKGFEIA
     RKRRKKLTSV DKANVLEVSA LWRQIVEEEK ENYPDVELEH LYIDNCAMQL VRRPTSFDVI
     VTGNIFGDIL SDEAGVVVGS LGMLPSASIG DRYALYEPVH GSAPDIAGKG IANPIATILS
     AAMMLKYSFN MDKAHDLIEK AIEETLNQGY RTPDIYSEGC IKVGTKEITD KILENLERLK
     DAYT
//