VDH_STRA4
ID VDH_STRA4 Reviewed; 364 AA.
AC O69056;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Valine dehydrogenase {ECO:0000303|PubMed:10612726};
DE Short=ValDH;
DE EC=1.4.1.23 {ECO:0000269|PubMed:10612726};
GN Name=vdh {ECO:0000303|PubMed:10612726};
OS Streptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 /
OS NBRC 107858).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1081613;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP MUTAGENESIS OF LYS-79 AND LYS-91.
RC STRAIN=ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858;
RX PubMed=10612726; DOI=10.1111/j.1574-6968.2000.tb08868.x;
RA Hyun C.-G., Kim S.S., Park K.-H., Suh J.-W.;
RT "Valine dehydrogenase from Streptomyces albus: gene cloning, heterologous
RT expression and identification of active site by site-directed
RT mutagenesis.";
RL FEMS Microbiol. Lett. 182:29-34(2000).
RN [2]
RP MUTAGENESIS OF ALA-124.
RC STRAIN=ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858;
RX PubMed=11386345; DOI=10.1023/a:1010245310057;
RA Hyun C.-G., Kim S.S., Lee I.H., Suh J.-W.;
RT "Alteration of substrate specificity of valine dehydrogenase from
RT Streptomyces albus.";
RL Antonie Van Leeuwenhoek 78:237-242(2000).
CC -!- FUNCTION: Oxidative deamination of branched-chain amino acids. Oxidizes
CC L-valine and L-alpha-aminobutyric acid efficiently, and L-alanine and
CC L-isoleucine less efficiently. D-valine and L-glutamate were not
CC substrates for the enzyme. The catabolism of valine is the major source
CC of fatty acid precursors for macrolide biosynthesis and a vital source
CC of antibiotic precursors. {ECO:0000269|PubMed:10612726}.
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:0000269|PubMed:10612726};
CC -!- ACTIVITY REGULATION: Inhibited by pyridoxal 5'-phosphate (PLP).
CC {ECO:0000269|PubMed:10612726}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 mM for L-valine {ECO:0000269|PubMed:10612726};
CC KM=0.133 mM for NAD(+) {ECO:0000269|PubMed:10612726};
CC KM=0.438 mM for 3-methyl-2-oxobutanoate
CC {ECO:0000269|PubMed:10612726};
CC KM=0.0576 mM for NADH {ECO:0000269|PubMed:10612726};
CC Note=kcat is 47.5 sec(-1) for the oxidative deamination of L-valine.
CC kcat is 314.5 sec(-1) for the reductive amination of 3-methyl-2-
CC oxobutanoate. {ECO:0000269|PubMed:10612726};
CC -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC {ECO:0000269|PubMed:10612726}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF061195; AAC16007.1; -; Genomic_DNA.
DR AlphaFoldDB; O69056; -.
DR SMR; O69056; -.
DR SABIO-RK; O69056; -.
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 1: Evidence at protein level;
KW Branched-chain amino acid catabolism; Cytoplasm; NAD; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..364
FT /note="Valine dehydrogenase"
FT /id="PRO_0000182810"
FT ACT_SITE 91
FT /evidence="ECO:0000305"
FT BINDING 191..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT MUTAGEN 79
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10612726"
FT MUTAGEN 91
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10612726"
FT MUTAGEN 124
FT /note="A->G: Displays lower activities toward aliphatic
FT amino acids, but higher activities toward L-phenylalanine,
FT L-tyrosine and L-methionine."
FT /evidence="ECO:0000269|PubMed:11386345"
SQ SEQUENCE 364 AA; 38398 MW; F33FBF2A3F1805FE CRC64;
MTDVTGAPAD VLHTLFHSDQ GGHEQVVLCQ DRASGLKAVI ALHSTALGPA LGGTRFYPYA
NEAEAVADAL NLARGMSYKN AMAGLEHGGG KAVIIGDPEQ IKSEELLLAY GRFVASLGGR
YVTACDVGTY VADMDVVARE CRWTTGRSPE NGGAGDSSVL TSFGVYQGMR AAAQHLWGDP
TLRDRTVGIA GVGKVGHHLV EHLLAEGAHV VVTDVRKDVV RSLTERHPSV VAVADTDALI
RVENLDIYAP CALGGALNDE TVPVLTAKVV CGAANNQLAH PGVEKDLADR GILYAPDYVV
NAGGVIQVAD ELHGFDFDRC KAKAAKIYDT TLAIFARAKE DGIPPAAAAD RIAEQRMAEA
RARR
