ID   DHLE_BACSU              Reviewed;         364 AA.
AC   P54531;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 150.
DE   RecName: Full=Leucine dehydrogenase;
DE            Short=LeuDH;
DE            EC=1.4.1.9;
GN   Name=yqiT; OrderedLocusNames=BSU24080;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- FUNCTION: Catalyzes the reversible deamination of L-leucine to 4-
CC       methyl-2-oxopentanoate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-leucine + NAD(+) + H2O = 4-methyl-2-oxopentanoate + NH4(+) +
CC         NADH + H(+); 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; D84432; BAA12595.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14339.1; -; Genomic_DNA.
DR   PIR; B69962; B69962.
DR   RefSeq; WP_003230309.1; NC_000964.3.
DR   AlphaFoldDB; P54531; -.
DR   SMR; P54531; -.
DR   FunCoup; P54531; 36.
DR   IntAct; P54531; 1.
DR   MINT; P54531; -.
DR   STRING; 224308.BSU24080; -.
DR   jPOST; P54531; -.
DR   PaxDb; 224308-BSU24080; -.
DR   EnsemblBacteria; CAB14339; CAB14339; BSU_24080.
DR   GeneID; 938670; -.
DR   KEGG; bsu:BSU24080; -.
DR   PATRIC; fig|224308.179.peg.2622; -.
DR   eggNOG; COG0334; Bacteria.
DR   InParanoid; P54531; -.
DR   OrthoDB; 9803297at2; -.
DR   PhylomeDB; P54531; -.
DR   BioCyc; BSUB:BSU24080-MONOMER; -.
DR   UniPathway; UPA00363; UER00858.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P54531; -.
DR   GO; GO:0050049; F:L-leucine dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006552; P:L-leucine catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01075; NAD_bind_Leu_Phe_Val_DH; 1.
DR   FunFam; 3.40.50.10860:FF:000010; Leucine dehydrogenase; 1.
DR   FunFam; 3.40.50.720:FF:000196; Leucine dehydrogenase; 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   3: Inferred from homology;
KW   Branched-chain amino acid catabolism; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..364
FT                   /note="Leucine dehydrogenase"
FT                   /id="PRO_0000182804"
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;  39992 MW;  4A40BA6735DDA2C8 CRC64;
     MELFKYMEKY DYEQLVFCQD EQSGLKAIIA IHDTTLGPAL GGTRMWTYEN EEAAIEDALR
     LARGMTYKNA AAGLNLGGGK TVIIGDPRKD KNEEMFRAFG RYIQGLNGRY ITAEDVGTTV
     EDMDIIHDET DYVTGISPAF GSSGNPSPVT AYGVYRGMKA AAKAAFGTDS LEGKTIAVQG
     VGNVAYNLCR HLHEEGANLI VTDINKQSVQ RAVEDFGARA VDPDDIYSQD CDIYAPCALG
     ATINDDTIKQ LKAKVIAGAA NNQLKETRHG DQIHEMGIVY APDYVINAGG VINVADELYG
     YNAERALKKV EGIYGNIERV LEISQRDGIP AYLAADRLAE ERIERMRRSR SQFLQNGHSV
     LSRR
//