ID   DHLE_BACLI              Reviewed;         364 AA.
AC   Q53560;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Leucine dehydrogenase;
DE            Short=LeuDH;
DE            EC=1.4.1.9;
GN   Name=ldh;
OS   Bacillus licheniformis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RC   STRAIN=TSN9;
RX   PubMed=8597545; DOI=10.1007/bf00169940;
RA   Nagata S., Bakthavatsalam S., Galkin A.G., Asada H., Sakai S., Esaki N.,
RA   Soda K., Ohshima T., Nagasaki S., Misono H.;
RT   "Gene cloning, purification, and characterization of thermostable and
RT   halophilic leucine dehydrogenase from a halophilic thermophile, Bacillus
RT   licheniformis TSN9.";
RL   Appl. Microbiol. Biotechnol. 44:432-438(1995).
CC   -!- FUNCTION: Catalyzes the reversible deamination of L-leucine to 4-
CC       methyl-2-oxopentanoate. Can also use other substrates such as L-
CC       isoleucine, L-valine and L-2-aminobutyrate. The 2-oxo analogs of
CC       branched-chain and straight-chain amino acids serve as good substrates
CC       for the reverse reaction. {ECO:0000269|PubMed:8597545}.
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:8597545};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.1 mM for L-leucine {ECO:0000269|PubMed:8597545};
CC         KM=3.3 mM for L-isoleucine {ECO:0000269|PubMed:8597545};
CC         KM=12.5 mM for L-valine {ECO:0000269|PubMed:8597545};
CC         KM=0.31 mM for NAD(+) {ECO:0000269|PubMed:8597545};
CC         KM=1 mM for 4-methyl-2-oxopentanoate {ECO:0000269|PubMed:8597545};
CC         KM=3.8 mM for 2-oxoisovalerate {ECO:0000269|PubMed:8597545};
CC         KM=2.4 mM for 2-oxovalerate {ECO:0000269|PubMed:8597545};
CC         KM=0.25 mM for NADH {ECO:0000269|PubMed:8597545};
CC         KM=330 mM for NH(3) {ECO:0000269|PubMed:8597545};
CC       pH dependence:
CC         Optimum pH is 10.3 for the oxidative deamination of L-leucine.
CC         {ECO:0000269|PubMed:8597545};
CC       Temperature dependence:
CC         Thermostable. Retains full activity on heating at 65 degrees Celsius
CC         for 1 hour, but loses the activity completely on heating at 70
CC         degrees Celsius for 1 hour. {ECO:0000269|PubMed:8597545};
CC   -!- PATHWAY: Amino-acid degradation; L-leucine degradation; 4-methyl-2-
CC       oxopentanoate from L-leucine (dehydrogenase route): step 1/1.
CC       {ECO:0000269|PubMed:8597545}.
CC   -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:8597545}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; S81735; AAB36205.1; -; Genomic_DNA.
DR   RefSeq; WP_003183340.1; NZ_UAQA01000025.1.
DR   AlphaFoldDB; Q53560; -.
DR   SMR; Q53560; -.
DR   GeneID; 76972619; -.
DR   PATRIC; fig|1402.62.peg.2762; -.
DR   OMA; TYVADMD; -.
DR   UniPathway; UPA00363; UER00858.
DR   GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR   GO; GO:0050049; F:leucine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01075; NAD_bind_Leu_Phe_Val_DH; 1.
DR   Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val/Trp_DH.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR016211; Glu/Phe/Leu/Val/Trp_DH_bac/arc.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42722; LEUCINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42722:SF1; VALINE DEHYDROGENASE; 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; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   1: Evidence at protein level;
KW   Branched-chain amino acid catabolism; NAD; Oxidoreductase.
FT   CHAIN           1..364
FT                   /note="Leucine dehydrogenase"
FT                   /id="PRO_0000182802"
FT   ACT_SITE        80
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   BINDING         180..186
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   364 AA;  40040 MW;  A13A967F6E84F873 CRC64;
     MELFRYMEQY DYEQLVFCQD KQSGLKAIIA IHDTTLGPAL GGTRMWTYES EEAAIEDALR
     LARGMTYKNA AAGLNLGGGK TVIIGDPRKD KNEEMFRAFG RYIQGLNGRY ITAEDVGTTV
     EDMDIIHDET DFVTGISPAF GSSGNPSPVT AYGVYKGMKA AAKAAFGTDS LEGKTVAVQG
     VGNVAYNLCR HLHEEGAKLI VTDINKEAVE RAVAEFGARA VDPDDIYSQE CDIYAPCALG
     ATINDDTIPQ LKAKVIAGAA NNQLKETRHG DQIHDMGIVY APDYVINAGG VINVADELYG
     YNSERALKKV EGIYGNIERV LEISKRDRIP TYLAADRLAE ERIERMRQSR SQFLQNGHHI
     LSRR
//