LEU3_MYCVP
ID LEU3_MYCVP Reviewed; 336 AA.
AC A1T6Z4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Mvan_2129;
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) 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: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; CP000511; ABM12944.1; -; Genomic_DNA.
DR RefSeq; WP_011779358.1; NC_008726.1.
DR AlphaFoldDB; A1T6Z4; -.
DR SMR; A1T6Z4; -.
DR STRING; 350058.Mvan_2129; -.
DR EnsemblBacteria; ABM12944; ABM12944; Mvan_2129.
DR KEGG; mva:Mvan_2129; -.
DR eggNOG; COG0473; Bacteria.
DR HOGENOM; CLU_031953_0_1_11; -.
DR OMA; EYDLGAR; -.
DR OrthoDB; 1551125at2; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000009159; 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_01035; LeuB_type2; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR023698; LeuB_actb.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 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; Reference proteome.
FT CHAIN 1..336
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_1000063878"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT BINDING 211
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT BINDING 271..283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT SITE 128
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
FT SITE 178
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01035"
SQ SEQUENCE 336 AA; 35569 MW; 43316F6F42B0B6FA CRC64;
MRLAVIAGDG IGPEVITEAL KVLDAVLPGV EKTEYDLGAR QYHKTGEVLP DSVLEELKGH
DAILLGAIGD PSVPSGLLER GLLLRIRFEL DHHINLRPAR LYPGVQSPLA GNPEIDFVVV
REGTEGPYTG NGGAIRVGTP HEIATEVSVN TAFGVRRAVQ DAFGRAQQRR KHLTLVHKNN
VLTNAGSLWW RTVQTVAAEY PDVEVAYQHV DAATIHMVTD PGRFDVIVTD NLFGDIITDL
AAAVCGGIGL AASGNIDATL THPSMFEPVH GSAPDIAGQG IADPTAAVMS VSLLLAHMAE
VDAAARVDKA VAEHLATRGD EKLSTAAVGE RILGKL
