ID   DHLE_BACCR              Reviewed;         366 AA.
AC   P0A392; Q59194;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Leucine dehydrogenase;
DE            Short=LeuDH;
DE            EC=1.4.1.9;
GN   Name=ldh; OrderedLocusNames=BC_4162;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
CC   -!- FUNCTION: Catalyzes the reversible deamination of L-leucine to 4-
CC       methyl-2-oxopentanoate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-leucine + NAD(+) = 4-methyl-2-oxopentanoate + H(+) +
CC         NADH + NH4(+); Xref=Rhea:RHEA:12220, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57427, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.9;
CC   -!- PATHWAY: Amino-acid degradation; L-leucine degradation; 4-methyl-2-
CC       oxopentanoate from L-leucine (dehydrogenase route): step 1/1.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; AE016877; AAP11078.1; -; Genomic_DNA.
DR   RefSeq; NP_833877.1; NC_004722.1.
DR   RefSeq; WP_000171355.1; NZ_CP034551.1.
DR   AlphaFoldDB; P0A392; -.
DR   SMR; P0A392; -.
DR   STRING; 226900.BC_4162; -.
DR   MetOSite; P0A392; -.
DR   EnsemblBacteria; AAP11078; AAP11078; BC_4162.
DR   GeneID; 67508802; -.
DR   KEGG; bce:BC4162; -.
DR   PATRIC; fig|226900.8.peg.4302; -.
DR   HOGENOM; CLU_025763_0_0_9; -.
DR   OMA; TYVADMD; -.
DR   BRENDA; 1.4.1.9; 648.
DR   UniPathway; UPA00363; UER00858.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0050049; F:leucine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR   InterPro; IPR016211; Glu/Phe/Leu/Val_DH_bac/arc.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42722; PTHR42722; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 2.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PIRSF; PIRSF000188; Phe_leu_dh; 1.
DR   PRINTS; PR00082; GLFDHDRGNASE.
DR   SMART; SM00839; ELFV_dehydrog; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Branched-chain amino acid catabolism; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..366
FT                   /note="Leucine dehydrogenase"
FT                   /id="PRO_0000182801"
FT   ACT_SITE        82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   BINDING         182..188
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   366 AA;  39867 MW;  DA84E58062E772AC CRC64;
     MTLEIFEYLE KYDYEQVVFC QDKESGLKAI IAIHDTTLGP ALGGTRMWTY DSEEAAIEDA
     LRLAKGMTYK NAAAGLNLGG AKTVIIGDPR KDKSEAMFRA LGRYIQGLNG RYITAEDVGT
     TVDDMDIIHE ETDFVTGISP SFGSSGNPSP VTAYGVYRGM KAAAKEAFGT DNLEGKVIAV
     QGVGNVAYHL CKHLHAEGAK LIVTDINKEA VQRAVEEFGA SAVEPNEIYG VECDIYAPCA
     LGATVNDETI PQLKAKVIAG SANNQLKEDR HGDIIHEMGI VYAPDYVINA GGVINVADEL
     YGYNRERALK RVESIYDTIA KVIEISKRDG IATYVAADRL AEERIASLKN SRSTYLRNGH
     DIISRR