LEU3_THET2
ID LEU3_THET2 Reviewed; 345 AA.
AC P61494; P00351;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=3-isopropylmalate dehydrogenase;
DE EC=1.1.1.85;
DE AltName: Full=3-IPM-DH;
DE AltName: Full=Beta-IPM dehydrogenase;
DE Short=IMDH;
GN Name=leuB; OrderedLocusNames=TT_C0867;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Miyazaki J., Kobashi N., Nishiyama M., Yamane H.;
RT "Characterization of homoisocitrate dehydrogenase from Thermus thermophilus
RT HB27 and the evolutionary importance of beta-decarboxylating
RT dehydrogenase.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(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 oxopentanoate
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate
CC + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.1.1.85;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 3/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. LeuB type 1 subfamily. {ECO:0000305}.
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DR EMBL; AB085839; BAB96756.1; -; Genomic_DNA.
DR EMBL; AE017221; AAS81211.1; -; Genomic_DNA.
DR RefSeq; WP_011173296.1; NC_005835.1.
DR AlphaFoldDB; P61494; -.
DR SMR; P61494; -.
DR STRING; 262724.TT_C0867; -.
DR EnsemblBacteria; AAS81211; AAS81211; TT_C0867.
DR KEGG; tth:TT_C0867; -.
DR eggNOG; COG0473; Bacteria.
DR HOGENOM; CLU_031953_0_3_0; -.
DR OMA; EYDLGAR; -.
DR OrthoDB; 1551125at2; -.
DR BRENDA; 1.1.1.85; 2305.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01033; LeuB_type1; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR004429; Isopropylmalate_DH.
DR PANTHER; PTHR42979; PTHR42979; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; 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; Cytoplasm;
KW Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD;
KW Oxidoreductase.
FT CHAIN 1..345
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083774"
FT BINDING 74..87
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 274..286
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 139
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT SITE 185
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 345 AA; 36750 MW; 38CDF736312B229E CRC64;
MKVAVLPGDG IGPEVTEAAL KVLRALDEAE GLGLAYEVFP FGGAAIDAFG EPFPEPTRKG
VEEAEAVLLG SVGGPKWDGL PRKIRPETGL LSLRKSQDLF ANLRPAKVFP GLERLSPLKE
EIARGVDVLI VRELTGGIYF GEPRGMSEAE AWNTERYSKP EVERVARVAF EAARKRRKHV
VSVDKANVLE VGEFWRKTVE EVGRGYPDVA LEHQYVDAMA MHLVRSPARF DVVVTGNIFG
DILSDLASVL PGSLGLLPSA SLGRGTPVFE PVHGSAPDIA GKGLANPTAA ILSAAMMLEH
AFGLVELARK VEDAVAKALL EAPPPDLGGS AGTEAFTATV LRHLA
