ID   VDH_STRCM               Reviewed;         358 AA.
AC   Q53872;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Valine dehydrogenase {ECO:0000250|UniProtKB:Q06539};
DE            Short=ValDH;
DE            EC=1.4.1.23 {ECO:0000250|UniProtKB:Q06539};
GN   Name=vdh;
OS   Streptomyces cinnamonensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces virginiae group.
OX   NCBI_TaxID=1900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3823.5;
RX   PubMed=8921870; DOI=10.1016/0378-1119(96)00305-8;
RA   Leiser A., Birch A., Robinson J.A.;
RT   "Cloning, sequencing, overexpression in Escherichia coli, and inactivation
RT   of the valine dehydrogenase gene in the polyether antibiotic producer
RT   Streptomyces cinnamonensis.";
RL   Gene 177:217-222(1996).
CC   -!- FUNCTION: Oxidative deamination of branched-chain amino acids. The
CC       catabolism of valine is the major source of fatty acid precursors for
CC       macrolide biosynthesis and a vital source of antibiotic precursors.
CC       {ECO:0000250|UniProtKB:Q06539}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-valine + NAD(+) = 3-methyl-2-oxobutanoate + H(+) +
CC         NADH + NH4(+); Xref=Rhea:RHEA:30763, ChEBI:CHEBI:11851,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57762, ChEBI:CHEBI:57945; EC=1.4.1.23;
CC         Evidence={ECO:0000250|UniProtKB:Q06539};
CC   -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC       {ECO:0000250|UniProtKB:Q06539}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q06539}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; U42212; AAC44587.1; -; Genomic_DNA.
DR   PIR; JC5176; JC5176.
DR   AlphaFoldDB; Q53872; -.
DR   SMR; Q53872; -.
DR   UniPathway; UPA00362; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043837; F:valine dehydrogenase (NAD) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006574; P:valine 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; 1.
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   3: Inferred from homology;
KW   Branched-chain amino acid catabolism; Cytoplasm; NAD; Oxidoreductase.
FT   CHAIN           1..358
FT                   /note="Valine dehydrogenase"
FT                   /id="PRO_0000182812"
FT   ACT_SITE        88
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   BINDING         188..194
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   358 AA;  37750 MW;  D629AB9518B0A74D CRC64;
     MTEADNGVLH TLFHSDQGGH EQVVLCQDRA SGLKAVIAIH STALGPALGG TRFYPYATEE
     EAVADVLNLS RGMSYKNAMA GLDHGGGKAV IIGDPEQIKS EDLLLAFGRF VASLGGRYVT
     ACDVGTYVAD MDVVARECRW TTGRSPENGG AGDSSVLTAF GVFQGMRASA EHLWGDPSLR
     GRKVGVAGVG KVGHHLVEHL LEDGADVVIT DVREESVNRS THKHPSVTAV ADTEALIRTE
     GLDIYAPCAL GGALDDDSVP VLTAKVVCGA ANNQLAHPGV EKDLADRSIL YAPDYVVNAG
     GVIQVADELR GFDFDRCKAK ASKIFDTTLA IFARAKEDGI PPAAAADRIA EQRMSDAR