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   16-JUN-2009, entry version 30.
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).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22608415; PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B.,
RA   Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A.,
RA   Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T.,
RA   Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D.,
RA   Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with
RT   Bacillus anthracis.";
RL   Nature 423:87-91(2003).
CC   -!- FUNCTION: Functions catabolically in the bacterial metabolism of
CC       branched-chain L-amino acids, and plays an important role in spore
CC       germination in cooperation with alanine dehydrogenase (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: L-leucine + H(2)O + NAD(+) = 4-methyl-2-
CC       oxopentanoate + NH(3) + NADH.
CC   -!- PATHWAY: Amino-acid degradation; L-leucine degradation; 4-methyl-
CC       2-oxopentanoic acid from L-leucine (dehydrogenase route): step
CC       1/1.
CC   -!- SUBUNIT: Homohexamer (By similarity).
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
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DR   EMBL; AE016877; AAP11078.1; -; Genomic_DNA.
DR   RefSeq; NP_833877.1; -.
DR   HSSP; Q59771; 1C1D.
DR   SMR; P0A392; 3-366.
DR   GeneID; 1206507; -.
DR   GenomeReviews; AE016877_GR; BC_4162.
DR   KEGG; bce:BC4162; -.
DR   HOGENOM; P0A392; -.
DR   OMA; P0A392; VDVYAPC.
DR   BioCyc; BCER226900:BC_4162-MON; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0050049; F:leucine dehydrogenase activity; IEA:EC.
DR   GO; GO:0009083; P:branched chain family amino acid catabolic ...; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer.
DR   InterPro; IPR016211; Glu/Phe/Leu/Val_DH_bac/arc.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PIRSF; PIRSF000188; Phe_leu_dh; 1.
DR   PRINTS; PR00082; GLFDHDRGNASE.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Branched-chain amino acid catabolism; Complete proteome; NAD;
KW   Oxidoreductase.
FT   CHAIN         1    366       Leucine dehydrogenase.
FT                                /FTId=PRO_0000182801.
FT   NP_BIND     182    188       NAD (Potential).
FT   ACT_SITE     82     82       By similarity.
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
//