ID   LEU3_ARCFU              Reviewed;         326 AA.
AC   O29627;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 63.
DE   RecName: Full=3-isopropylmalate dehydrogenase;
DE            Short=3-IPM-DH;
DE            Short=IMDH;
DE            EC=1.1.1.85;
DE   AltName: Full=Beta-IPM dehydrogenase;
GN   Name=leuB; OrderedLocusNames=AF_0628;
OS   Archaeoglobus fulgidus.
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; Archaeoglobus.
OX   NCBI_TaxID=2234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
RX   MEDLINE=98049343; PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
RA   Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
RA   Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
RA   Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
RA   Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
RA   Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
RA   Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
RA   Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
RA   Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
RA   Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
RA   Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-
RT   reducing archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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DR   EMBL; AE000782; AAB90611.1; -; Genomic_DNA.
DR   PIR; D69328; D69328.
DR   RefSeq; NP_069462.1; -.
DR   HSSP; P00351; 1XAA.
DR   GeneID; 1483846; -.
DR   GenomeReviews; AE000782_GR; AF_0628.
DR   KEGG; afu:AF0628; -.
DR   NMPDR; fig|224325.1.peg.621; -.
DR   TIGR; AF_0628; -.
DR   HOGENOM; O29627; -.
DR   OMA; O29627; TCAHKAN.
DR   BioCyc; AFUL224325:AF_0628-MON; -.
DR   BRENDA; 1.1.1.85; 7576.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:EC.
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:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR   InterPro; IPR011828; LEU3_arc.
DR   Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1.
DR   PANTHER; PTHR11835; IDH_IMDH_dimeric; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   TIGRFAMs; TIGR02088; LEU3_arch; 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    326       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083808.
FT   NP_BIND     255    267       NAD (By similarity).
FT   METAL       198    198       Magnesium or manganese (By similarity).
FT   METAL       222    222       Magnesium or manganese (By similarity).
FT   METAL       226    226       Magnesium or manganese (By similarity).
FT   BINDING      81     81       Substrate (By similarity).
FT   BINDING      91     91       Substrate (By similarity).
FT   BINDING     112    112       Substrate (By similarity).
FT   BINDING     198    198       Substrate (By similarity).
FT   SITE        119    119       Important for catalysis (By similarity).
FT   SITE        165    165       Important for catalysis (By similarity).
SQ   SEQUENCE   326 AA;  35819 MW;  4B3BE727572CF0A9 CRC64;
     MKKIVVIPGD GIGKEVMEAA MLILEKLDLP FEYSYYDAGD EALEKYGKAL PDETLEACRK
     SDAVLFGAAG ETAADVIVRL RRELGTFANV RPAKAIEGIE CLYPGLDIVV VRENTECLYM
     GFEFGFGDVT EAIRVITREA SERIARYAFE LAKREGRKKV TALHKANVMK KTCGLFRDVC
     REVAKDYPEI QYNDYYIDAA CMYLVMDPFR FDVIVTTNMF GDIVSDLAAG LVGGLGLAPS
     ANVGERTAIF EPVHGAAFDI AGKGIANPTA MILTACMMLR HFGYVEEAKK VEEAVEKTIK
     EGKKTPDLGG NLKTMEFANE VASLLD
//