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LEU3_RHOJR
ID   LEU3_RHOJR              Reviewed;         336 AA.
AC   Q0S2H1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 112.
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};
GN   OrderedLocusNames=RHA1_ro06490;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG98265.1; -; Genomic_DNA.
DR   RefSeq; WP_011598375.1; NC_008268.1.
DR   AlphaFoldDB; Q0S2H1; -.
DR   SMR; Q0S2H1; -.
DR   STRING; 101510.RHA1_ro06490; -.
DR   EnsemblBacteria; ABG98265; ABG98265; RHA1_ro06490.
DR   KEGG; rha:RHA1_ro06490; -.
DR   PATRIC; fig|101510.16.peg.6545; -.
DR   eggNOG; COG0473; Bacteria.
DR   HOGENOM; CLU_031953_0_1_11; -.
DR   OMA; EYDLGAR; -.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000008710; 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_1000063879"
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;  35328 MW;  F927E59A61C742F8 CRC64;
     MKLAVIPGDG IGVEVTAEAL KVLRKLVPDL QTTEYDLGAR RYNATGELLP DADLAAIREH
     DAILLGAIGD PSVTPGVLER GLLLNMRFAL DHHVNLRPSQ LYPGSKSPLA AQPDIDFVVV
     REGTEGPYTG NGGAIRVGTP HEIATEVSIN TWFGAERVVR YAFALAQTRR KHVTLIHKTN
     VLSNAGAIWT RAVETVSAEY PDVETAYCHI DAATIYMVTD PSRFDVIVTD NLFGDIITDL
     AGAVTGGIGL AASGNIDASG TNPSMFEPVH GSAPDIAGQG IADPTAAILS AALLLRHLGR
     DGDAARIEAA VEADLASRGD SKVVTSEVGD RIAAAL
 
 
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