ID   LEU3_ASHGO              Reviewed;         372 AA.
AC   O60027;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 60.
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=LEU2; OrderedLocusNames=AAL012C;
OS   Ashbya gossypii (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=33169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10895 / NRRL Y-1056 / CBS 109.51;
RA   Mohr C., Philippsen P.;
RT   "Isolation of the Ashbya gossypii LEU2 gene and its use as a marker
RT   gene in transformation experiments.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10895 / NRRL Y-1056 / CBS 109.51;
RA   Revuelta J.L.;
RT   "AgLEU2 gene.";
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / NRRL Y-1056 / CBS 109.51;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient
RT   Saccharomyces cerevisiae genome.";
RL   Science 304:304-307(2004).
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.
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DR   EMBL; AJ006406; CAA07006.1; -; Genomic_DNA.
DR   EMBL; AJ001115; CAA04541.1; -; Genomic_DNA.
DR   EMBL; AE016814; AAS50354.1; -; Genomic_DNA.
DR   RefSeq; NP_982530.1; -.
DR   HSSP; P12010; 2AYQ.
DR   GeneID; 4618651; -.
DR   KEGG; ago:AGOS_AAL012C; -.
DR   NMPDR; fig|33169.1.peg.175; -.
DR   AGD; AAL012C; -.
DR   HOGENOM; O60027; -.
DR   OMA; O60027; LPGDHIG.
DR   BioCyc; AGOS-XXX-01:AGOS-XXX-01-000175-MON; -.
DR   BRENDA; 1.1.1.85; 279361.
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; 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    372       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083598.
FT   NP_BIND      79     90       NAD (By similarity).
FT   NP_BIND     289    300       NAD (By similarity).
FT   METAL       225    225       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      97     97       Substrate (By similarity).
FT   BINDING     107    107       Substrate (By similarity).
FT   BINDING     136    136       Substrate (By similarity).
FT   BINDING     225    225       Substrate (By similarity).
FT   SITE        143    143       Important for catalysis (By similarity).
FT   SITE        192    192       Important for catalysis (By similarity).
SQ   SEQUENCE   372 AA;  39309 MW;  84C96C221B0C438D CRC64;
     MAAVKRIVVL PGDHIGREVV EEAVKVLGAV EQSLSDVHFD FQYHLVGGAA IDATGSALPD
     EALGAAKEAD AVLLGAVGGP KWQGGAVRPE QGLLKLRQEL GVYANLRPCN FAADSLLELS
     PLRPEIARDT DIMVVRELLG GSYFGERHED EGDGVAWDTD KYTVKEVQRI ARMAGFLALQ
     HDPPLPVWSL DKANVLASSR LWRKTVEETF QSEFPNVQLQ HQLIDSAAMI LVKNPRAFNG
     VVVTSNMFGD IISDEASVIP GSLGLLPSAS LASLPDSKSA FGLYEPCHGS APDLPAGKAN
     PIGCILSAAM MLKLSLNMVA AGEAVEQAVQ EVLDSGVRTG DLLGSSSTSE VGDAIALAVK
     EALRRQSAAG LS
//