ID   VDH_STRFR               Reviewed;         371 AA.
AC   P40176;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 94.
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 fradiae (Streptomyces roseoflavus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C373.1;
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; L33872; AAA62388.1; -; Genomic_DNA.
DR   RefSeq; WP_043463560.1; NZ_MCNU01000058.1.
DR   AlphaFoldDB; P40176; -.
DR   SMR; P40176; -.
DR   STRING; 1906.SFRA_10720; -.
DR   eggNOG; COG0334; Bacteria.
DR   OMA; TYVADMD; -.
DR   SABIO-RK; P40176; -.
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   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..371
FT                   /note="Valine dehydrogenase"
FT                   /id="PRO_0000182814"
FT   ACT_SITE        95
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   BINDING         200..206
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   371 AA;  38767 MW;  6CE3197FCD0CC41A CRC64;
     MTDASHPTAA DDLGALSTLF RSEQGGHERV LLCQDRESGL KAVIALHSTA LGPALGGTRF
     HAYASDEEAV LDALNLARGM SYKNALAGLP HGGGKAVIIG SPAPVSEGGL KSEALLRAYG
     RFVASLDGRY VTACDVGTYV ADMDVVAREC RWTTGRSPEN GGAGDSSVLT AFGVFQGMRA
     SAQALWGEPT LRGRTVGVAG VGKVGHHLVD HLVEDGARVV VTDVRPESVE RVRARHPRVV
     AVPDTESLIR ADLDVYAPCA LGGALNDDTV PALTARVVCG AANNQLAHPG VEKDLAGRGI
     LYAPDYVVNA GGVIQVADEL LGFDFDRAKA KAAQIFDTTL AIFDRARTDG VPPAVAADRI
     AEQRMAEART V