LEU3_LEPIN
ID LEU3_LEPIN Reviewed; 358 AA.
AC P24015;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 138.
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=LA_2152;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Kenniwicki / Serogroup Pomona / Serovar pomona;
RX PubMed=8336106; DOI=10.1099/00221287-139-5-1093;
RA Ding M., Yelton D.B.;
RT "Cloning and analysis of the leuB gene of Leptospira interrogans serovar
RT pomona.";
RL J. Gen. Microbiol. 139:1093-1103(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
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; M59431; AAA72088.1; -; Unassigned_DNA.
DR EMBL; AE010300; AAN49351.1; -; Genomic_DNA.
DR RefSeq; NP_712333.1; NC_004342.2.
DR RefSeq; WP_000799846.1; NC_004342.2.
DR AlphaFoldDB; P24015; -.
DR SMR; P24015; -.
DR STRING; 189518.LA_2152; -.
DR EnsemblBacteria; AAN49351; AAN49351; LA_2152.
DR GeneID; 61141667; -.
DR KEGG; lil:LA_2152; -.
DR PATRIC; fig|189518.3.peg.2144; -.
DR HOGENOM; CLU_031953_0_3_12; -.
DR InParanoid; P24015; -.
DR OMA; EYDLGAR; -.
DR BioCyc; MetaCyc:MON-11898; -.
DR BRENDA; 1.1.1.85; 2986.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000001408; Chromosome I.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..358
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083702"
FT BINDING 75..88
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 283..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 142
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT SITE 192
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 358 AA; 38871 MW; E64192745EB9C370 CRC64;
MKNVAVLSGD GIGPEVMEIA ISVLKKALGA KVSEFQFKEG FVGGIAIDKT GHPLPPETLK
LCEESSAILF GSVGGPKWET LPPEKQPERG ALLPLRKHFD LFANLRPAII YPELKNASPV
RSDIIGNGLD ILILRELTGG IYFGQPKGRE GSGQEEFAYD TMKYSRREIE RIAKVAFQAA
RKRNNKVTSI DKANVLTTSV FWKEVVIELH KKEFSDVQLN HLYVDNAAMQ LIVNPKQFDV
VLCENMFGDI LSDEASIITG SIGMLPSASL SESGFGLYEP SGGSAPDIAG KGVANPIAQV
LSAALMLRYS FSMEEEANKI ETAVRKTIAS GKRTRDIAEV GSTIVGTKEI GQLIESFL