DHLE_BACCE
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 03-AUG-2022, entry version 81.
DE RecName: Full=Leucine dehydrogenase;
DE Short=LeuDH;
DE EC=1.4.1.9;
GN Name=ldh;
OS Bacillus cereus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1396;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-18; 47-56;
RP 160-192; 214-254 AND 279-298, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=DSM 626 / NCIMB 11796 / T;
RX 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 gene
RT from Bacillus cereus.";
RL J. Biotechnol. 54:77-80(1997).
CC -!- FUNCTION: Catalyzes the reversible deamination of L-leucine to 4-
CC methyl-2-oxopentanoate. {ECO:0000269|PubMed:9188201}.
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 Evidence={ECO:0000269|PubMed:9188201};
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; U51099; AAA96314.1; -; Genomic_DNA.
DR RefSeq; WP_000171355.1; NZ_WBPO01000030.1.
DR AlphaFoldDB; P0A393; -.
DR SMR; P0A393; -.
DR STRING; 1396.DJ87_697; -.
DR GeneID; 67508802; -.
DR eggNOG; COG0334; Bacteria.
DR OMA; TYVADMD; -.
DR UniPathway; UPA00363; UER00858.
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 1: Evidence at protein level;
KW Branched-chain amino acid catabolism; Direct protein sequencing; NAD;
KW Oxidoreductase.
FT CHAIN 1..366
FT /note="Leucine dehydrogenase"
FT /id="PRO_0000182800"
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
