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   16-JUN-2009, entry version 65.
DE   RecName: Full=Leucine dehydrogenase;
DE            Short=LeuDH;
DE            EC=1.4.1.9;
GN   Name=yqiT; OrderedLocusNames=BSU24080;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   MEDLINE=97124195; PubMed=8969508;
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
RT   the Bacillus subtilis genome containing the skin element and many
RT   sporulation genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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: 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; D84432; BAA12595.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14339.1; -; Genomic_DNA.
DR   PIR; B69962; B69962.
DR   RefSeq; NP_390288.1; -.
DR   HSSP; Q59771; 1C1D.
DR   SMR; P54531; 1-364.
DR   GeneID; 938670; -.
DR   GenomeReviews; AL009126_GR; BSU24080.
DR   KEGG; bsu:BSU24080; -.
DR   NMPDR; fig|224308.1.peg.2412; -.
DR   SubtiList; BG11723; yqiT.
DR   HOGENOM; P54531; -.
DR   OMA; P54531; VDVYAPC.
DR   BioCyc; BSUB224308:BSU2406-MON; -.
DR   BRENDA; 1.4.1.9; 150.
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    364       Leucine dehydrogenase.
FT                                /FTId=PRO_0000182804.
FT   NP_BIND     180    186       NAD (Potential).
FT   ACT_SITE     80     80       By similarity.
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
//