ID A0A0M4M099_9ACTN Unreviewed; 338 AA.
AC A0A0M4M099;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01035};
DE EC=1.1.1.85 {ECO:0000256|HAMAP-Rule:MF_01035};
DE AltName: Full=3-IPM-DH {ECO:0000256|HAMAP-Rule:MF_01035};
DE AltName: Full=Beta-IPM dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01035};
DE Short=IMDH {ECO:0000256|HAMAP-Rule:MF_01035};
GN Name=leuB {ECO:0000256|HAMAP-Rule:MF_01035};
GN ORFNames=AL705_01355 {ECO:0000313|EMBL:ALE19557.1};
OS Lawsonella clevelandensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Lawsonellaceae;
OC Lawsonella.
OX NCBI_TaxID=1528099 {ECO:0000313|EMBL:ALE19557.1, ECO:0000313|Proteomes:UP000068137};
RN [1] {ECO:0000313|EMBL:ALE19557.1, ECO:0000313|Proteomes:UP000068137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X1698 {ECO:0000313|EMBL:ALE19557.1,
RC ECO:0000313|Proteomes:UP000068137};
RX PubMed=26659691;
RA Nicholson A.C., Bell M., Humrighouse B.W., McQuiston J.R.;
RT "Complete Genome Sequences for Two Strains of a Novel Fastidious, Partially
RT Acid-Fast, Gram-Positive Corynebacterineae Bacterium, Derived from Human
RT Clinical Samples.";
RL Genome Announc. 3:e01462-15(2015).
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_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;
CC Evidence={ECO:0000256|ARBA:ARBA00000624, ECO:0000256|HAMAP-
CC Rule:MF_01035};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01035};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01035};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01035};
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|HAMAP-
CC Rule:MF_01035}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01035}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01035}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. LeuB type 2 subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01035}.
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DR EMBL; CP012390; ALE19557.1; -; Genomic_DNA.
DR RefSeq; WP_053962634.1; NZ_LR584267.1.
DR AlphaFoldDB; A0A0M4M099; -.
DR STRING; 1528099.AL705_01355; -.
DR GeneID; 84894279; -.
DR KEGG; cbq:AL705_01355; -.
DR PATRIC; fig|1528099.3.peg.279; -.
DR OrthoDB; 5289857at2; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000068137; 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 Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR HAMAP; MF_01035; LeuB_type2; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR023698; LeuB_actb.
DR PANTHER; PTHR43275; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR PANTHER; PTHR43275:SF1; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 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|HAMAP-Rule:MF_01035};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|HAMAP-Rule:MF_01035};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01035};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430, ECO:0000256|HAMAP-
KW Rule:MF_01035}; Magnesium {ECO:0000256|HAMAP-Rule:MF_01035};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01035};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01035};
KW NAD {ECO:0000256|HAMAP-Rule:MF_01035};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01035,
KW ECO:0000313|EMBL:ALE19557.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000068137}.
FT DOMAIN 2..333
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 272..284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT SITE 129
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT SITE 179
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
SQ SEQUENCE 338 AA; 35916 MW; D38051B6754E60EC CRC64;
MNLAVIGGDG IGPEVTAEAL KVLHTVVPNI EVTDYALGAD HYLETGEILS DETVESIRQQ
DAILLGAIGD PARVAPGVLE RGLLLKLRFA LDHFVNLRPA KLYAGVESPL AGNPALDFVV
VREGTEGLYC GDGGAIRVGT PAEVATETSL NTRFGVERVV RDAFERAMKR NKRLTLVHKM
NVLTNAGSLW KRTVDEVSVE YPEVTTDYCH IDACTIYMVT DPGRFDVIVT DNLFGDIITD
LAGAVMGGIG LAASGNIDAT RTNPSMFEPV HGSAPDIAGK GLADPTAAII SAAMLLEHLG
YDEEATRIMQ VVEEDVAHRG DGPISTSAVG DRIVAALQ
//
