Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P42709 (VDH_STRAM) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Valine dehydrogenase

Short name=ValDH
EC=1.4.1.-
Gene names
Name:vdh
OrganismStreptomyces ambofaciens
Taxonomic identifier1889 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length106 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Oxidative deamination of branched-chain amino acids. The catabolism of valine is the major source of fatty acid precursors for macrolide biosynthesis and a vital source of antibiotic precursors.

Catalytic activity

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

Pathway

Amino-acid degradation; L-valine degradation.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Ontologies

Keywords
   Biological processBranched-chain amino acid catabolism
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological_processvaline catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – ›106›105Valine dehydrogenase
PRO_0000182811

Sites

Active site911 By similarity

Experimental info

Non-terminal residue1061

Sequences

Sequence LengthMass (Da)Tools
P42709 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 1A1116020A884ADE

FASTA10610,964
        10         20         30         40         50         60 
MTDVTGAPAD VLHTLFHSDQ GGHEQVVLCQ DRASGLKAVI ALHSTALGPA LGGTRFYPIA 

        70         80         90        100 
NEAEAVADAL NLARGMSYKN AMAGLEHGGG KAVIIGDPEQ IKSEEL 

« Hide

References

[1]"Amino acid catabolism and antibiotic synthesis: valine is a source of precursors for macrolide biosynthesis in Streptomyces ambofaciens and Streptomyces fradiae."
Tang L., Zhang Y.X., Hutchinson C.R.
J. Bacteriol. 176:6107-6119(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 15154 / NBRC 13685 / NRRL 2420 / Isolate B3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L33871 Genomic DNA. Translation: AAA62597.1.

3D structure databases

ProteinModelPortalP42709.
SMRP42709. Positions 23-106.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00362.

Family and domain databases

InterProIPR006095. Glu/Leu/Phe/Val_DH.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR016211. Glu/Phe/Leu/Val_DH_bac/arc.
[Graphical view]
PANTHERPTHR11606:SF3. PTHR11606:SF3. 1 hit.
PfamPF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PROSITEPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVDH_STRAM
AccessionPrimary (citable) accession number: P42709
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways