ID   LEU3_ANASP              Reviewed;         362 AA.
AC   Q8YXA2;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   16-JUN-2009, entry version 43.
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=alr1313;
OS   Anabaena sp. (strain PCC 7120).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=21595285; PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T.,
RA   Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M.,
RA   Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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; BA000019; BAB73270.1; -; Genomic_DNA.
DR   PIR; AF1970; AF1970.
DR   RefSeq; NP_485356.1; -.
DR   HSSP; Q56268; 1A05.
DR   GeneID; 1104908; -.
DR   GenomeReviews; BA000019_GR; alr1313.
DR   KEGG; ana:alr1313; -.
DR   NMPDR; fig|103690.1.peg.1623; -.
DR   HOGENOM; Q8YXA2; -.
DR   OMA; Q8YXA2; EAFDTMR.
DR   BioCyc; NSP103690:ALR1313-MON; -.
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    362       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083628.
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;  38769 MW;  E414E8BCC353E6D0 CRC64;
     MTQNYRITLL PGDGIGPEIM AVAVDVLKVV GQQFDIQFDF QEALIGGAAI DATGEPLPSA
     TLDTCRHSDA VLLAAIGGYK WDSLPPHQRP EGGLLGLRAG LELFANLRPA QILPQLIDAS
     TLKREVVEGV DIMVVRELTG GIYFGKPRGI FTTETGEKRG VNTMVYTESE IDRIGRIAFE
     TARKRRGKLC SVDKANVLDV SQLWRDRITN LSQEYPDVEL SHLYVDNAAM QLVRAPKQFD
     TIVTGNLFGD ILSDAAAMLT GSIGMLPSAS LGASGPGVFE PVHGSAPDIA GQDKANPLAQ
     VLSAAMMLRY ALDQPQAADK IEQAVLQVLE QGDRTGDIIS VGMNLLGCRG MGDSLIKALA
     KS
//