LEU3_BACFR
ID LEU3_BACFR Reviewed; 353 AA.
AC P54354;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=BF3444;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=8569539; DOI=10.1111/j.1348-0421.1995.tb02238.x;
RA Sarker M.R., Akimoto S., Ugai H., Kuwahara T., Ohnishi Y.;
RT "Nucleotide sequence of the gene encoding beta-isopropylmalate
RT dehydrogenase (leuB) from Bacteroides fragilis.";
RL Microbiol. Immunol. 39:525-529(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(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; D45169; BAA08117.1; -; Genomic_DNA.
DR EMBL; AP006841; BAD50187.1; -; Genomic_DNA.
DR PIR; I40235; I40235.
DR RefSeq; WP_005789841.1; NZ_UYXF01000038.1.
DR RefSeq; YP_100721.1; NC_006347.1.
DR AlphaFoldDB; P54354; -.
DR SMR; P54354; -.
DR STRING; 295405.BF3444; -.
DR EnsemblBacteria; BAD50187; BAD50187; BF3444.
DR GeneID; 66331921; -.
DR KEGG; bfr:BF3444; -.
DR PATRIC; fig|295405.11.peg.3308; -.
DR HOGENOM; CLU_031953_0_3_10; -.
DR OMA; EYDLGAR; -.
DR BRENDA; 1.1.1.85; 755.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000002197; 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..353
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083644"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 142
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT SITE 187
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 353 AA; 39098 MW; 355259EA221F4A84 CRC64;
MDFKIAVLAG DGIGPEISVQ GVEVMSAVCE KFGHKVNYEY AICGADAIDK VGDPFPEETY
RVCKNADAVL FSAVGDPKFD NDPTAKVRPE QGLLAMRKKL GLFANIRPVQ TFKCLVHKSP
LRAELVEGAD FLCIRELTGG MYFGEKYQDN DKAYDTNMYT RPEIERILKV GFEYAMKRRK
HLTVVDKANV LASSRLWRQI AQEMAPQYPE VTTDYMFVDN AAMKMIQEPK FFDVMVTENT
FGDILTDEGS VISGSMGLLP SASTGESTPV FEPIHGSWPQ AKGLNIANPL AQILSVAMLF
EYFDCKAEGA LIRKAVDASL DANVRTPEIQ VEGGEKFGTK EVGAWIVDYI RKA
