ID   VDH_STRAM               Reviewed;         106 AA.
AC   P42709;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Valine dehydrogenase {ECO:0000250|UniProtKB:Q06539};
DE            Short=ValDH;
DE            EC=1.4.1.23 {ECO:0000250|UniProtKB:Q06539};
DE   Flags: Fragment;
GN   Name=vdh;
OS   Streptomyces ambofaciens.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1889;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15154 / NBRC 13685 / NRRL 2420 / Isolate B3;
RX   PubMed=7928973; DOI=10.1128/jb.176.19.6107-6119.1994;
RA   Tang L., Zhang Y.X., Hutchinson C.R.;
RT   "Amino acid catabolism and antibiotic synthesis: valine is a source of
RT   precursors for macrolide biosynthesis in Streptomyces ambofaciens and
RT   Streptomyces fradiae.";
RL   J. Bacteriol. 176:6107-6119(1994).
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; L33871; AAA62597.1; -; Genomic_DNA.
DR   AlphaFoldDB; P42709; -.
DR   SMR; P42709; -.
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; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR   InterPro; IPR016211; Glu/Phe/Leu/Val_DH_bac/arc.
DR   PANTHER; PTHR42722; PTHR42722; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..>106
FT                   /note="Valine dehydrogenase"
FT                   /id="PRO_0000182811"
FT   ACT_SITE        91
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   NON_TER         106
SQ   SEQUENCE   106 AA;  10964 MW;  1A1116020A884ADE CRC64;
     MTDVTGAPAD VLHTLFHSDQ GGHEQVVLCQ DRASGLKAVI ALHSTALGPA LGGTRFYPIA
     NEAEAVADAL NLARGMSYKN AMAGLEHGGG KAVIIGDPEQ IKSEEL