LEU3_PRIM3
ID LEU3_PRIM3 Reviewed; 369 AA.
AC P41019; D5DLN0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=3-isopropylmalate dehydrogenase;
DE EC=1.1.1.85;
DE AltName: Full=3-IPM-DH;
DE AltName: Full=Beta-IPM dehydrogenase;
DE Short=IMDH;
GN Name=leuB; Synonyms=leuC; OrderedLocusNames=BMD_4682;
OS Priestia megaterium (strain DSM 319 / IMG 1521) (Bacillus megaterium).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=592022;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7764969; DOI=10.1007/bf00221230;
RA Meinhardt F., Busskamp M., Wittchen K.D.;
RT "Cloning and sequencing of the leu C and npr M genes and a putative spo IV
RT gene from Bacillus megaterium DSM319.";
RL Appl. Microbiol. Biotechnol. 41:344-351(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 319 / IMG 1521;
RX PubMed=21705586; DOI=10.1128/jb.00449-11;
RA Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA Koenig S.S., Creasy H.H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA Bremer E., Jahn D., Ravel J., Vary P.S.;
RT "Genome sequences of the biotechnologically important Bacillus megaterium
RT strains QM B1551 and DSM319.";
RL J. Bacteriol. 193:4199-4213(2011).
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 (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 3/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. LeuB type 1 subfamily. {ECO:0000305}.
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DR EMBL; X65184; CAA46295.1; -; Genomic_DNA.
DR EMBL; CP001982; ADF41506.1; -; Genomic_DNA.
DR PIR; I40226; I40226.
DR RefSeq; WP_013085139.1; NC_014103.1.
DR AlphaFoldDB; P41019; -.
DR SMR; P41019; -.
DR EnsemblBacteria; ADF41506; ADF41506; BMD_4682.
DR KEGG; bmd:BMD_4682; -.
DR PATRIC; fig|592022.4.peg.4680; -.
DR HOGENOM; CLU_031953_0_3_9; -.
DR OMA; EYDLGAR; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000002365; 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_01033; LeuB_type1; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR004429; Isopropylmalate_DH.
DR PANTHER; PTHR42979; PTHR42979; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00169; leuB; 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.
FT CHAIN 1..369
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083641"
FT BINDING 76..89
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 281..293
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 141
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT SITE 191
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 13..24
FT /note="VGTEVTKGAVAV -> GQSNQRRCCR (in Ref. 1; CAA46295)"
FT /evidence="ECO:0000305"
FT CONFLICT 32..33
FT /note="FD -> LR (in Ref. 1; CAA46295)"
FT /evidence="ECO:0000305"
FT CONFLICT 53..57
FT /note="TPLPE -> SSSSR (in Ref. 1; CAA46295)"
FT /evidence="ECO:0000305"
FT CONFLICT 64..65
FT /note="KQ -> NE (in Ref. 1; CAA46295)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="N -> F (in Ref. 1; CAA46295)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="E -> D (in Ref. 1; CAA46295)"
FT /evidence="ECO:0000305"
FT CONFLICT 173..176
FT /note="RQAF -> ASI (in Ref. 1; CAA46295)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="A -> AA (in Ref. 1; CAA46295)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="A -> V (in Ref. 1; CAA46295)"
FT /evidence="ECO:0000305"
FT CONFLICT 368..369
FT /note="YS -> SR (in Ref. 1; CAA46295)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 40024 MW; FCEE79332E08F3AB CRC64;
MTKKVAVLPG DGVGTEVTKG AVAVLKAIGE RFDHQFEFTY GLIGGAAIDE AGTPLPESTI
ETCKQADAVL LGSVGGPKWD RNPSHLRPEK GLLAIRKELD LYANLRPVTF YDSLADASPL
KKEYIEGVDF IIVRELTGGL YFGKPSERRT EGNKETVVDT LFYKRTEIER IIRQAFDTAV
NRRKKVTSVD KANVLESSRV WREVAEEVAK DYPDVELEHM LVDSAAMQLI RNPKYFDVVV
TENMFGDILS DEASMLTGSL GMLPSASLTA DGPSLYEPVH GSAPDIAGQN KANPIAAILS
AAMLLRHSFG LEKEAAVIEQ AVESVLHAGH RTADLADGNH YLGTDKMVEA ITAVIANDSA
ISSIMTAYS
