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Protein

Valine dehydrogenase

Gene

vdh

Organism
Streptomyces ambofaciens
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei91 – 911PROSITE-ProRule annotation

GO - Molecular functioni

  1. oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor Source: InterPro

GO - Biological processi

  1. valine catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Branched-chain amino acid catabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00362.

Names & Taxonomyi

Protein namesi
Recommended name:
Valine dehydrogenase (EC:1.4.1.-)
Short name:
ValDH
Gene namesi
Name:vdh
OrganismiStreptomyces ambofaciens
Taxonomic identifieri1889 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – ›106›105Valine dehydrogenasePRO_0000182811Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP42709.
SMRiP42709. Positions 23-106.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR006095. Glu/Leu/Phe/Val_DH.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR016211. Glu/Phe/Leu/Val_DH_bac/arc.
[Graphical view]
PANTHERiPTHR11606:SF3. PTHR11606:SF3. 1 hit.
PfamiPF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

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

P42709-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTDVTGAPAD VLHTLFHSDQ GGHEQVVLCQ DRASGLKAVI ALHSTALGPA
60 70 80 90 100
LGGTRFYPIA NEAEAVADAL NLARGMSYKN AMAGLEHGGG KAVIIGDPEQ

IKSEEL
Length:106
Mass (Da):10,964
Last modified:January 23, 2007 - v2
Checksum:i1A1116020A884ADE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei106 – 1061

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L33871 Genomic DNA. Translation: AAA62597.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L33871 Genomic DNA. Translation: AAA62597.1.

3D structure databases

ProteinModelPortaliP42709.
SMRiP42709. Positions 23-106.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00362.

Family and domain databases

InterProiIPR006095. Glu/Leu/Phe/Val_DH.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR016211. Glu/Phe/Leu/Val_DH_bac/arc.
[Graphical view]
PANTHERiPTHR11606:SF3. PTHR11606:SF3. 1 hit.
PfamiPF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiVDH_STRAM
AccessioniPrimary (citable) accession number: P42709
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 64 of the entry and version 2 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

External Data

Dasty 3

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 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.