ID   LEU3_ANAVT              Reviewed;         362 AA.
AC   Q3M8T9;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   04-NOV-2008, entry version 25.
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=Ava_2987;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
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; CP000117; ABA22597.1; -; Genomic_DNA.
DR   RefSeq; YP_323492.1; -.
DR   GeneID; 3681222; -.
DR   GenomeReviews; CP000117_GR; Ava_2987.
DR   KEGG; ava:Ava_2987; -.
DR   NMPDR; fig|240292.3.peg.2045; -.
DR   HOGENOM; Q3M8T9; -.
DR   BioCyc; AVAR240292:AVA_2987-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    362       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000250100.
FT   NP_BIND      78     91       NAD (By similarity).
FT   NP_BIND     284    296       NAD (By similarity).
FT   METAL       226    226       Magnesium or manganese (By similarity).
FT   METAL       250    250       Magnesium or manganese (By similarity).
FT   METAL       254    254       Magnesium or manganese (By similarity).
FT   BINDING      98     98       Substrate (By similarity).
FT   BINDING     108    108       Substrate (By similarity).
FT   BINDING     136    136       Substrate (By similarity).
FT   BINDING     226    226       Substrate (By similarity).
FT   SITE        143    143       Important for catalysis (By similarity).
FT   SITE        194    194       Important for catalysis (By similarity).
SQ   SEQUENCE   362 AA;  38849 MW;  F95CB20C7827D793 CRC64;
     MTQNYRITLL PGDGIGPEIM AVAVDVLKVV GQQFDIQFDF QEALIGGAAI DATGEPLPSA
     TLDTCRQSDA VLLAAIGGYK WDSLPPHQRP EGGLLGLRAG LELFANLRPA QILPQLIDAS
     TLKREVVEGV DIMVVRELTG GIYFGKPRGI FTTETGEKRG VNTMVYTESE IDRIGRIAFE
     TARKRRGKLC SVDKANVLDV SQLWRDRITK LSQEYPDVEL SHLYVDNAAM QLVRAPKQFD
     TIVTGNLFGD ILSDAAAMLT GSIGMLPSAS LGASGPGVFE PVHGSAPDIA GLDKANPLAQ
     VLSAAMMLRY ALNQPQAADK IEQAVLQVLE QGDRTGDIMS VGMNLLGCRA MGDSLIKALE
     KS
//