VDH_STRCO
ID VDH_STRCO Reviewed; 364 AA.
AC Q06539; Q9RKJ7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Valine dehydrogenase;
DE Short=ValDH;
DE EC=1.4.1.23 {ECO:0000269|PubMed:2324704};
GN Name=vdh; OrderedLocusNames=SCO4089; ORFNames=SCD25.25c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21.
RC STRAIN=A3(2) / J802;
RX PubMed=8320231; DOI=10.1128/jb.175.13.4176-4185.1993;
RA Tang L., Hutchinson C.R.;
RT "Sequence, transcriptional, and functional analyses of the valine
RT (branched-chain amino acid) dehydrogenase gene of Streptomyces
RT coelicolor.";
RL J. Bacteriol. 175:4176-4185(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [3]
RP CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=2324704; DOI=10.1099/00221287-136-2-273;
RA Navarette R.M., Vara J.A., Hutchinson C.R.;
RT "Purification of an inducible L-valine dehydrogenase of Streptomyces
RT coelicolor A3(2).";
RL J. Gen. Microbiol. 136:273-281(1990).
CC -!- FUNCTION: Oxidative deamination of branched-chain amino acids. Oxidizes
CC L-valine and L-alpha-aminobutyric acid efficiently, and L-isoleucine
CC and L-leucine less efficiently. Does not act on D-valine. The
CC catabolism of L-valine is the major source of fatty acid precursors for
CC macrolide biosynthesis and a vital source of antibiotic precursors.
CC Uses NAD; no activity was found with NADP.
CC {ECO:0000269|PubMed:2324704}.
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:2324704};
CC -!- ACTIVITY REGULATION: Repressed in minimal medium by the presence of
CC glucose and NH4(+), glycerol and NH4(+), or glycerol and asparagine.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 10.5 with valine as substrate.
CC {ECO:0000269|PubMed:2324704};
CC -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:2324704}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By valine.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
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DR EMBL; L13455; AAA71983.1; -; Genomic_DNA.
DR EMBL; AL939118; CAB56369.1; -; Genomic_DNA.
DR PIR; B40657; B40657.
DR RefSeq; NP_628270.1; NC_003888.3.
DR RefSeq; WP_011029424.1; NZ_VNID01000030.1.
DR AlphaFoldDB; Q06539; -.
DR SMR; Q06539; -.
DR STRING; 100226.SCO4089; -.
DR GeneID; 1099526; -.
DR KEGG; sco:SCO4089; -.
DR PATRIC; fig|100226.15.peg.4148; -.
DR eggNOG; COG0334; Bacteria.
DR HOGENOM; CLU_025763_0_0_11; -.
DR InParanoid; Q06539; -.
DR OMA; TYVADMD; -.
DR PhylomeDB; Q06539; -.
DR BioCyc; MetaCyc:MON-17657; -.
DR UniPathway; UPA00362; -.
DR Proteomes; UP000001973; Chromosome.
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; Direct protein sequencing;
KW NAD; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8320231"
FT CHAIN 2..364
FT /note="Valine dehydrogenase"
FT /id="PRO_0000182813"
FT ACT_SITE 91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT BINDING 191..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT CONFLICT 20
FT /note="Q -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="A -> V (in Ref. 1; AAA71983)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 38309 MW; 80E8432B9FF645B4 CRC64;
MTDVNGAPAD VLHTLFHSDQ GGHEQVVLCQ DRASGLKAVI ALHSTALGPA LGGTRFYPYA
SEAEAVADAL NLARGMSYKN AMAGLDHGGG KAVIIGDPEQ IKSEELLLAY GRFVASLGGR
YVTACDVGTY VADMDVVARE CRWTTGRSPE NGGAGDSSVL TSFGVYQGMR AAAQHLWGDP
TLRDRTVGIA GVGKVGHHLV EHLLAEGAHV VVTDVRKDVV RGITERHPSV VAVADTDALI
RVENLDIYAP CALGGALNDD TVPVLTAKVV CGAANNQLAH PGVEKDLADR GILYAPDYVV
NAGGVIQVAD ELHGFDFDRC KAKASKIYDT TLAIFARAKE DGIPPAAAAD RIAEQRMAEA
RPRP
