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Protein

PEP-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL

Gene

dhaL

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone (PubMed:11350937). DhaL-ADP is converted to DhaL-ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone binds to DhaK (PubMed:11350937). DhaL acts also as coactivator of the transcription activator DhaR by binding to the sensor domain of DhaR (PubMed:15616579). In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity (PubMed:15616579). In the absence of dihydroxyacetone, DhaL-ADP is converted by the PTS to DhaL-ATP, which does not bind to DhaR (PubMed:15616579).2 Publications

Miscellaneous

Unlike the carbohydrate-specific transporters of the PTS, the complex DhaKML has no transport activity.Curated
The tightly bound ADP participates in a double displacement phosphoryl transfer reaction and thus plays the same role as histidines, cysteines and aspartic acids in other phosphoprotein intermediates.1 Publication

Catalytic activityi

Phosphoenolpyruvate + glycerone = pyruvate + glycerone phosphate.By similarity

Cofactori

Mg2+3 Publications

Temperature dependencei

Complexation with ADP increases the thermal unfolding temperature from 40 to 65 degrees Celsius.1 Publication

Pathwayi: glycerol degradation

This protein is involved in the pathway glycerol degradation, which is part of Polyol metabolism.Curated
View all proteins of this organism that are known to be involved in the pathway glycerol degradation and in Polyol metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi30MagnesiumCombined sources2 Publications1
Metal bindingi35MagnesiumCombined sources3 Publications1
Metal bindingi37MagnesiumCombined sources3 Publications1
Binding sitei121ADP; via carbonyl oxygenCombined sources3 Publications1
Binding sitei130ADP; via amide nitrogenCombined sources3 Publications1
Binding sitei178ADPCombined sources1 Publication1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi38 – 41ADPCombined sources3 Publications4
Nucleotide bindingi79 – 80ADPCombined sources3 Publications2
Nucleotide bindingi191 – 193ADPCombined sources3 Publications3

GO - Molecular functioni

  • ADP binding Source: EcoCyc
  • ATP binding Source: UniProtKB
  • glycerone kinase activity Source: InterPro
  • magnesium ion binding Source: UniProtKB
  • phosphoenolpyruvate-glycerone phosphotransferase activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionKinase, Transferase
Biological processGlycerol metabolism
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:MONOMER0-1261.
MetaCyc:MONOMER0-1261.
BRENDAi2.7.1.29. 2026.
UniPathwayiUPA00616.

Protein family/group databases

MoonProtiP76014.

Names & Taxonomyi

Protein namesi
Recommended name:
PEP-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL1 Publication (EC:2.7.1.121By similarity)
Gene namesi
Name:dhaL1 Publication
Synonyms:ycgS
Ordered Locus Names:b1199, JW5186
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13900. dhaL.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001215301 – 210PEP-dependent dihydroxyacetone kinase, ADP-binding subunit DhaLAdd BLAST210

Proteomic databases

PaxDbiP76014.
PRIDEiP76014.

Expressioni

Inductioni

Activated by DhaR.2 Publications

Interactioni

Subunit structurei

Homodimer (PubMed:16647083, PubMed:21209328, PubMed:24440518). The dihydroxyacetone kinase complex is composed of a homodimer of DhaM, a homodimer of DhaK and the subunit DhaL (PubMed:16647083, PubMed:21209328). DhaL also forms a complex with DhaR (PubMed:24440518).3 Publications

Protein-protein interaction databases

BioGridi4260762. 3 interactors.
DIPiDIP-11562N.
STRINGi316385.ECDH10B_1252.

Structurei

Secondary structure

1210
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 4Combined sources3
Helixi5 – 21Combined sources17
Helixi23 – 32Combined sources10
Beta strandi34 – 36Combined sources3
Helixi38 – 52Combined sources15
Helixi54 – 56Combined sources3
Helixi61 – 73Combined sources13
Helixi80 – 95Combined sources16
Beta strandi99 – 102Combined sources4
Helixi103 – 121Combined sources19
Beta strandi127 – 129Combined sources3
Helixi131 – 146Combined sources16
Helixi151 – 168Combined sources18
Helixi169 – 171Combined sources3
Helixi178 – 186Combined sources9
Helixi192 – 208Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BTDX-ray2.60A1-210[»]
3PNLX-ray2.20B2-210[»]
4LRZX-ray2.32A/B/C/D2-210[»]
ProteinModelPortaliP76014.
SMRiP76014.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP76014.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 206DhaLPROSITE-ProRule annotationAdd BLAST201

Phylogenomic databases

eggNOGiENOG4108UTZ. Bacteria.
COG2376. LUCA.
HOGENOMiHOG000226525.
InParanoidiP76014.
KOiK05879.
PhylomeDBiP76014.

Family and domain databases

InterProiView protein in InterPro
IPR012737. DhaK_L_YcgS.
IPR004007. DhaL_dom.
PfamiView protein in Pfam
PF02734. Dak2. 1 hit.
SMARTiView protein in SMART
SM01120. Dak2. 1 hit.
SUPFAMiSSF101473. SSF101473. 1 hit.
TIGRFAMsiTIGR02365. dha_L_ycgS. 1 hit.
PROSITEiView protein in PROSITE
PS51480. DHAL. 1 hit.

Sequencei

Sequence statusi: Complete.

P76014-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSRTQIVN WLTRCGDIFS TESEYLTGLD REIGDADHGL NMNRGFSKVV
60 70 80 90 100
EKLPAIADKD IGFILKNTGM TLLSSVGGAS GPLFGTFFIR AAQATQARQS
110 120 130 140 150
LTLEELYQMF RDGADGVISR GKAEPGDKTM CDVWVPVVES LRQSSEQNLS
160 170 180 190 200
VPVALEAASS IAESAAQSTI TMQARKGRAS YLGERSIGHQ DPGATSVMFM
210
MQMLALAAKE
Length:210
Mass (Da):22,632
Last modified:May 30, 2000 - v3
Checksum:i91C668A3E792CB5F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74283.1.
AP009048 Genomic DNA. Translation: BAA36056.2.
PIRiD64866.
RefSeqiNP_415717.1. NC_000913.3.
WP_000059411.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74283; AAC74283; b1199.
BAA36056; BAA36056; BAA36056.
GeneIDi945748.
KEGGiecj:JW5186.
eco:b1199.
PATRICifig|1411691.4.peg.1086.

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.

Entry informationi

Entry nameiDHAL_ECOLI
AccessioniPrimary (citable) accession number: P76014
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: July 5, 2017
This is version 131 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references