ID A0A1B2HYV7_9PSEU Unreviewed; 345 AA.
AC A0A1B2HYV7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=BBK82_21460 {ECO:0000313|EMBL:ANZ42918.1};
OS Lentzea guizhouensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=1586287 {ECO:0000313|EMBL:ANZ42918.1, ECO:0000313|Proteomes:UP000093053};
RN [1] {ECO:0000313|EMBL:ANZ42918.1, ECO:0000313|Proteomes:UP000093053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHS C013 {ECO:0000313|EMBL:ANZ42918.1,
RC ECO:0000313|Proteomes:UP000093053};
RA Cao C.;
RT "Complete genome sequence of the Lentzea guizhouensis DHS C013.";
RL Submitted (JUL-2016) 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_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; CP016793; ANZ42918.1; -; Genomic_DNA.
DR RefSeq; WP_065921241.1; NZ_CP016793.1.
DR AlphaFoldDB; A0A1B2HYV7; -.
DR STRING; 1586287.BBK82_21460; -.
DR KEGG; led:BBK82_21460; -.
DR OrthoDB; 5289857at2; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000093053; 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 Reference proteome {ECO:0000313|Proteomes:UP000093053}.
FT DOMAIN 2..334
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT BINDING 121
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 128
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 345 AA; 36829 MW; 40777B2B937B0B4F CRC64;
MRLAVIPGDG IGPEVIAEAL KVLNEVVPAA EITRYDLGAA RWHATGELLP ESVLGELRQH
DAILLGAVGD PSVPSGILER GLLLRLRFEL DHHVNLRPAR LYPGVRSPLA DPPEIDMVVV
REGTEGPYAG NGGLLRKDTP HEIATEVSIN TSFGVERVVR DAFARASNRQ RRHLTLVHKT
NVLTHAGSLW SRVVEEVSLQ HPDVTVAYQH VDAATIHMVT DPGRYDVIVT DNLFGDILTD
LAAAVTGGIG LAASGNMDVT RRNPSMFEPV HGSAPDIAGQ GIADPTAAVL SVALLLDHLG
EHEAARRIEA SVAFDLATRD HQSPGATYGI GDRLAALVSS NVRTG
//
