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Protein

Valine dehydrogenase

Gene

vdh

Organism
Streptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Oxidative deamination of branched-chain amino acids. Oxidizes L-valine and L-alpha-aminobutyric acid efficiently, and L-valine and L-isoleucine less efficiently. D-valine and L-glutamate were not substrates for the enzyme. The catabolism of valine is the major source of fatty acid precursors for macrolide biosynthesis and a vital source of antibiotic precursors.

Catalytic activityi

L-valine + H2O + NAD+ = 3-methyl-2-oxobutanoate + NH3 + NADH.

Enzyme regulationi

Inhibited by PLP.

Pathwayi: L-valine degradation

This protein is involved in the pathway L-valine degradation, which is part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the pathway L-valine degradation and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei91 – 911Curated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi191 – 1977NADSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Branched-chain amino acid catabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

SABIO-RKO69056.
UniPathwayiUPA00362.

Names & Taxonomyi

Protein namesi
Recommended name:
Valine dehydrogenase (EC:1.4.1.-)
Short name:
ValDH
Gene namesi
Name:vdh
OrganismiStreptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858)
Taxonomic identifieri1081613 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi79 – 791K → A: Loss of activity. 1 Publication
Mutagenesisi91 – 911K → A: Loss of activity. 1 Publication
Mutagenesisi124 – 1241A → G: Displays lower activities toward aliphatic amino acids, but higher activities toward L-phenylalanine, L-tyrosine and L-methionine. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 364363Valine dehydrogenasePRO_0000182810Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliO69056.
SMRiO69056. Positions 17-364.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. Glu/Leu/Phe/Val_DH.
IPR033524. Glu/Leu/Phe/Val_DH_AS.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR016211. Glu/Phe/Leu/Val_DH_bac/arc.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11606:SF3. PTHR11606:SF3. 1 hit.
PfamiPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000188. Phe_leu_dh. 1 hit.
PRINTSiPR00082. GLFDHDRGNASE.
SMARTiSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O69056-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDVTGAPAD VLHTLFHSDQ GGHEQVVLCQ DRASGLKAVI ALHSTALGPA
60 70 80 90 100
LGGTRFYPYA NEAEAVADAL NLARGMSYKN AMAGLEHGGG KAVIIGDPEQ
110 120 130 140 150
IKSEELLLAY GRFVASLGGR YVTACDVGTY VADMDVVARE CRWTTGRSPE
160 170 180 190 200
NGGAGDSSVL TSFGVYQGMR AAAQHLWGDP TLRDRTVGIA GVGKVGHHLV
210 220 230 240 250
EHLLAEGAHV VVTDVRKDVV RSLTERHPSV VAVADTDALI RVENLDIYAP
260 270 280 290 300
CALGGALNDE TVPVLTAKVV CGAANNQLAH PGVEKDLADR GILYAPDYVV
310 320 330 340 350
NAGGVIQVAD ELHGFDFDRC KAKAAKIYDT TLAIFARAKE DGIPPAAAAD
360
RIAEQRMAEA RARR
Length:364
Mass (Da):38,398
Last modified:January 23, 2007 - v3
Checksum:iF33FBF2A3F1805FE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061195 Genomic DNA. Translation: AAC16007.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061195 Genomic DNA. Translation: AAC16007.1.

3D structure databases

ProteinModelPortaliO69056.
SMRiO69056. Positions 17-364.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00362.
SABIO-RKO69056.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. Glu/Leu/Phe/Val_DH.
IPR033524. Glu/Leu/Phe/Val_DH_AS.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR016211. Glu/Phe/Leu/Val_DH_bac/arc.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11606:SF3. PTHR11606:SF3. 1 hit.
PfamiPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000188. Phe_leu_dh. 1 hit.
PRINTSiPR00082. GLFDHDRGNASE.
SMARTiSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Valine dehydrogenase from Streptomyces albus: gene cloning, heterologous expression and identification of active site by site-directed mutagenesis."
    Hyun C.-G., Kim S.S., Park K.-H., Suh J.-W.
    FEMS Microbiol. Lett. 182:29-34(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF LYS-79 AND LYS-91.
    Strain: ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858.
  2. "Alteration of substrate specificity of valine dehydrogenase from Streptomyces albus."
    Hyun C.-G., Kim S.S., Lee I.H., Suh J.-W.
    Antonie Van Leeuwenhoek 78:237-242(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ALA-124.
    Strain: ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858.

Entry informationi

Entry nameiVDH_STRA4
AccessioniPrimary (citable) accession number: O69056
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 86 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.