ID A0A099W8B1_9LIST Unreviewed; 350 AA.
AC A0A099W8B1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01033};
DE EC=1.1.1.85 {ECO:0000256|HAMAP-Rule:MF_01033};
DE AltName: Full=3-IPM-DH {ECO:0000256|HAMAP-Rule:MF_01033};
DE AltName: Full=Beta-IPM dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01033};
DE Short=IMDH {ECO:0000256|HAMAP-Rule:MF_01033};
GN Name=leuB {ECO:0000256|HAMAP-Rule:MF_01033,
GN ECO:0000313|EMBL:MBC1560648.1};
GN ORFNames=EP57_09025 {ECO:0000313|EMBL:KGL40688.1}, HB902_01100
GN {ECO:0000313|EMBL:MBC1560648.1};
OS Listeria booriae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1552123 {ECO:0000313|EMBL:KGL40688.1, ECO:0000313|Proteomes:UP000029844};
RN [1] {ECO:0000313|EMBL:KGL40688.1, ECO:0000313|Proteomes:UP000029844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL A5-0281 {ECO:0000313|EMBL:KGL40688.1,
RC ECO:0000313|Proteomes:UP000029844};
RA den Bakker H.C.;
RT "Novel Listeriaceae from food processing environments.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBC1560648.1, ECO:0000313|Proteomes:UP000541955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL L7-1387 {ECO:0000313|EMBL:MBC1560648.1,
RC ECO:0000313|Proteomes:UP000541955};
RA Liao J., Wiedmann M.;
RT "Soil Listeria distribution.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01033, ECO:0000256|RuleBase:RU004445}.
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 Evidence={ECO:0000256|ARBA:ARBA00000624, ECO:0000256|HAMAP-
CC Rule:MF_01033, ECO:0000256|RuleBase:RU004445};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01033,
CC ECO:0000256|RuleBase:RU004445};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01033,
CC ECO:0000256|RuleBase:RU004445};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01033, ECO:0000256|RuleBase:RU004445};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 3/4. {ECO:0000256|ARBA:ARBA00004762,
CC ECO:0000256|HAMAP-Rule:MF_01033, ECO:0000256|RuleBase:RU004445}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01033, ECO:0000256|RuleBase:RU004445}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01033}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. LeuB type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00008319, ECO:0000256|HAMAP-Rule:MF_01033}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01033}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGL40688.1}.
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DR EMBL; JNFA01000023; KGL40688.1; -; Genomic_DNA.
DR EMBL; JAARRW010000001; MBC1560648.1; -; Genomic_DNA.
DR RefSeq; WP_036085894.1; NZ_UGPF01000002.1.
DR AlphaFoldDB; A0A099W8B1; -.
DR STRING; 1552123.EP57_09025; -.
DR GeneID; 58717514; -.
DR eggNOG; COG0473; Bacteria.
DR OrthoDB; 9806254at2; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000029844; Unassembled WGS sequence.
DR Proteomes; UP000541955; Unassembled WGS sequence.
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 Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
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 NCBIfam; TIGR00169; leuB; 1.
DR PANTHER; PTHR42979; 3-ISOPROPYLMALATE DEHYDROGENASE; 1.
DR PANTHER; PTHR42979:SF1; 3-ISOPROPYLMALATE DEHYDROGENASE; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01033};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|HAMAP-Rule:MF_01033};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01033};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430, ECO:0000256|HAMAP-
KW Rule:MF_01033};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01033};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_01033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01033};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01033}; Reference proteome {ECO:0000313|Proteomes:UP000029844}.
FT DOMAIN 4..342
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT BINDING 275..287
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT SITE 139
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT SITE 185
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
SQ SEQUENCE 350 AA; 37572 MW; A377F66EFE05C2E4 CRC64;
MSYSITALPG DGIGPEIMAS GLEILETLAA KFQLDFTIET HPFGGAGIDA HSDPLPDATL
AACQKADAIL LGAIGGPKWD DAPKRPEQGL LALRKALGLF ANIRPIQVPA SITHLSPLKQ
EIVEGTDFIV VRELTGGIYF GEPKHWDENG AVDTLTYTAA EIERIAVQAF ELAKTRRNKV
TSVDKANVLA SSKLWRQIVE QVATRYPEVT LEHLYVDAAA MILIQRPTTF DVIVTENMFG
DILSDEASVL TGSLGMLPSA SHPESGPSLY EPIHGSAPDI AGQDIANPMS MISSISMMLR
QSFQLFEAAD YLDQAAADTM AAGFLTKDLG GDTSTTNFTK EVKKRVKGGE
//
