LEU3_BIFLD
ID LEU3_BIFLD Reviewed; 343 AA.
AC B3DTF8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01035};
DE EC=1.1.1.85 {ECO:0000255|HAMAP-Rule:MF_01035};
DE AltName: Full=3-IPM-DH {ECO:0000255|HAMAP-Rule:MF_01035};
DE AltName: Full=Beta-IPM dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01035};
DE Short=IMDH {ECO:0000255|HAMAP-Rule:MF_01035};
GN Name=leuB {ECO:0000255|HAMAP-Rule:MF_01035}; OrderedLocusNames=BLD_0981;
OS Bifidobacterium longum (strain DJO10A).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=205913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJO10A;
RX PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT reveals loci susceptible to deletion during pure culture growth.";
RL BMC Genomics 9:247-247(2008).
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 {ECO:0000255|HAMAP-Rule:MF_01035}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01035};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01035};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01035};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01035};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 3/4. {ECO:0000255|HAMAP-
CC Rule:MF_01035}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01035}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01035}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. LeuB type 2 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01035}.
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DR EMBL; CP000605; ACD98427.1; -; Genomic_DNA.
DR RefSeq; WP_007051335.1; NZ_AABM02000002.1.
DR AlphaFoldDB; B3DTF8; -.
DR SMR; B3DTF8; -.
DR EnsemblBacteria; ACD98427; ACD98427; BLD_0981.
DR GeneID; 66504643; -.
DR KEGG; blj:BLD_0981; -.
DR HOGENOM; CLU_031953_0_1_11; -.
DR OMA; EYDLGAR; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000002419; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01035; LeuB_type2; 1.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR023698; LeuB_actb.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 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..343
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_1000135854"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT BINDING 278..290
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT SITE 135
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT SITE 185
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
SQ SEQUENCE 343 AA; 37246 MW; 143417C91B926D30 CRC64;
MAKTYKIAVI PGDGIGKEVT PWAQKALEKA AEGVADFEYE NFDLGAERYL RDGAILPEDE
EERIKANDAI LLGAVGDPRI KAGILERGLL LKLRFDLDQY VNLRPSKLYK GVTSPLANPG
DIDFVVVREG TEGLYCGAGG AVRRNTPQEV ATEVSINTAY GVERVVRYAF KLAMKRKKHV
TLVHKKNVLV NAGDMWQRIV DKVGEEYPEV THDYQHIDAA TIFLVSDPSR FDVILTDNLF
GDILTDEAGS VVGGVGYSAS GCINASDEFP SMFEPIHGSA PDIAGQNKAN PTAAILSAAM
LLEHLGFDDA AKKIHTAVEA DIEELGSTVR STDQVGKDIL ARM
