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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: 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 – 911PROSITE-ProRule annotation

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

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 lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy 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

InterProiIPR033524. Glu/Leu/Phe/Val_DH_AS.
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

InterProiIPR033524. Glu/Leu/Phe/Val_DH_AS.
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...

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: July 6, 2016
This is version 70 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

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.