Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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. DhaL-ADP receives a phosphoryl group from DhaM and transmits it to dihydroxyacetone. DhaL-ADP acts also as a coactivator by binding to the sensor domain of DhaR. DhaL-ATP is inactive.1 Publication

Pathwayi: glycerol degradation

This protein is involved in the pathway glycerol degradation, which is part of Polyol metabolism.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei121 – 1211ADP; via carbonyl oxygen1 Publication
Binding sitei178 – 1781ADP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi35 – 417ADP1 Publication
Nucleotide bindingi79 – 802ADP1 Publication
Nucleotide bindingi191 – 1933ADP1 Publication

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycerol metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:MONOMER0-1261.
ECOL316407:JW5186-MONOMER.
MetaCyc:MONOMER0-1261.
RETL1328306-WGS:GSTH-4273-MONOMER.
BRENDAi2.7.1.29. 2026.
UniPathwayiUPA00616.

Protein family/group databases

MoonProtiP76014.

Names & Taxonomyi

Protein namesi
Recommended name:
PEP-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL (EC:2.7.-.-)
Gene namesi
Name:dhaL1 Publication
Synonyms:ycgS
Ordered Locus Names:b1199, JW5186
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13900. dhaL.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 210210PEP-dependent dihydroxyacetone kinase, ADP-binding subunit DhaLPRO_0000121530Add
BLAST

Proteomic databases

EPDiP76014.
PaxDbiP76014.
PRIDEiP76014.

Interactioni

Subunit structurei

The dihydroxyacetone kinase complex is composed of a homodimer of DhaM, a homodimer of DhaK and the subunit DhaL.1 Publication

Protein-protein interaction databases

BioGridi4260762. 3 interactions.
DIPiDIP-11562N.
STRINGi511145.b1199.

Structurei

Secondary structure

1
210
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 43Combined sources
Helixi5 – 2117Combined sources
Helixi23 – 3210Combined sources
Beta strandi34 – 363Combined sources
Helixi38 – 5215Combined sources
Helixi54 – 563Combined sources
Helixi61 – 7313Combined sources
Helixi80 – 9516Combined sources
Beta strandi99 – 1024Combined sources
Helixi103 – 12119Combined sources
Beta strandi127 – 1293Combined sources
Helixi131 – 14616Combined sources
Helixi151 – 16818Combined sources
Helixi169 – 1713Combined sources
Helixi178 – 1869Combined sources
Helixi192 – 20817Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP76014.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 206201DhaLPROSITE-ProRule annotationAdd
BLAST

Domaini

The DhaL subunit corresponds to the C-terminal part of ATP-dependent dihydroxykinases and the DhaK subunit corresponds to the N-terminal part.

Sequence similaritiesi

Contains 1 DhaL domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108UTZ. Bacteria.
COG2376. LUCA.
HOGENOMiHOG000226525.
InParanoidiP76014.
KOiK05879.
OMAiGENVDRG.
OrthoDBiEOG65J57G.
PhylomeDBiP76014.

Family and domain databases

InterProiIPR012737. DhaK_L_YcgS.
IPR004007. DhaL_dom.
[Graphical view]
PfamiPF02734. Dak2. 1 hit.
[Graphical view]
SMARTiSM01120. Dak2. 1 hit.
[Graphical view]
SUPFAMiSSF101473. SSF101473. 1 hit.
TIGRFAMsiTIGR02365. dha_L_ycgS. 1 hit.
PROSITEiPS51480. DHAL. 1 hit.
[Graphical view]

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.
PATRICi32117648. VBIEscCol129921_1246.

Cross-referencesi

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.

3D structure databases

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

Protein-protein interaction databases

BioGridi4260762. 3 interactions.
DIPiDIP-11562N.
STRINGi511145.b1199.

Protein family/group databases

MoonProtiP76014.

Proteomic databases

EPDiP76014.
PaxDbiP76014.
PRIDEiP76014.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74283; AAC74283; b1199.
BAA36056; BAA36056; BAA36056.
GeneIDi945748.
KEGGiecj:JW5186.
eco:b1199.
PATRICi32117648. VBIEscCol129921_1246.

Organism-specific databases

EchoBASEiEB3659.
EcoGeneiEG13900. dhaL.

Phylogenomic databases

eggNOGiENOG4108UTZ. Bacteria.
COG2376. LUCA.
HOGENOMiHOG000226525.
InParanoidiP76014.
KOiK05879.
OMAiGENVDRG.
OrthoDBiEOG65J57G.
PhylomeDBiP76014.

Enzyme and pathway databases

UniPathwayiUPA00616.
BioCyciEcoCyc:MONOMER0-1261.
ECOL316407:JW5186-MONOMER.
MetaCyc:MONOMER0-1261.
RETL1328306-WGS:GSTH-4273-MONOMER.
BRENDAi2.7.1.29. 2026.

Miscellaneous databases

EvolutionaryTraceiP76014.
PROiP76014.

Family and domain databases

InterProiIPR012737. DhaK_L_YcgS.
IPR004007. DhaL_dom.
[Graphical view]
PfamiPF02734. Dak2. 1 hit.
[Graphical view]
SMARTiSM01120. Dak2. 1 hit.
[Graphical view]
SUPFAMiSSF101473. SSF101473. 1 hit.
TIGRFAMsiTIGR02365. dha_L_ycgS. 1 hit.
PROSITEiPS51480. DHAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography."
    Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.
    Electrophoresis 20:2181-2195(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: B / BL21.
  5. "The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor."
    Gutknecht R., Beutler R., Garcia-Alles L.F., Baumann U., Erni B.
    EMBO J. 20:2480-2486(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "From ATP as substrate to ADP as coenzyme: functional evolution of the nucleotide binding subunit of dihydroxyacetone kinases."
    Baechler C., Fluekiger-Bruehwiler K., Schneider P., Baehler P., Erni B.
    J. Biol. Chem. 280:18321-18325(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE OF ADP.
  7. "Crystal structure of the nucleotide-binding subunit DhaL of the Escherichia coli dihydroxyacetone kinase."
    Oberholzer A.E., Schneider P., Baumann U., Erni B.
    J. Mol. Biol. 359:539-545(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ADP AND MAGNESIUM IONS.

Entry informationi

Entry nameiDHAL_ECOLI
AccessioniPrimary (citable) accession number: P76014
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: May 11, 2016
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Unlike the carbohydrate-specific transporters of the PTS, the complex DhaKML has no transport activity.
Complexation with ADP increases the thermal unfolding temperature from 40 to 65 degrees Celsius. 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.

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
  4. 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.