ID   DHLE_BACCE              Reviewed;         366 AA.
AC   P0A393; Q59194;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Leucine dehydrogenase;
DE            Short=LeuDH;
DE            EC=1.4.1.9;
GN   Name=ldh;
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-18;
RP   47-56; 160-192; 214-254 AND 279-298.
RC   STRAIN=DSM 626;
RX   MEDLINE=97331894; PubMed=9188201; DOI=10.1016/S0168-1656(97)01670-2;
RA   Stoyan T., Recktenwald A., Kula M.R.;
RT   "Cloning, sequencing and overexpression of the leucine dehydrogenase
RT   gene from Bacillus cereus.";
RL   J. Biotechnol. 54:77-80(1997).
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; U51099; AAA96314.1; -; Genomic_DNA.
DR   HSSP; Q59771; 1C1D.
DR   SMR; P0A393; 3-366.
DR   BRENDA; 1.4.1.9; 604.
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   1: Evidence at protein level;
KW   Branched-chain amino acid catabolism; Direct protein sequencing; NAD;
KW   Oxidoreductase.
FT   CHAIN         1    366       Leucine dehydrogenase.
FT                                /FTId=PRO_0000182800.
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
//