PTS-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL

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P76014 (DHAL_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 102. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
PTS-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL
EC=2.7.-.-

Gene names

Name:	dhaL
Synonyms:	ycgS
Ordered Locus Names:	b1199, JW5186

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	210 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for phosphorylating 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. Ref.5
Pathway	Polyol metabolism; glycerol degradation.
Subunit structure	The dihydroxyacetone kinase complex is composed of a homodimer of DhaM, a homodimer of DhaK and the subunit DhaL.
Domain	The DhaL subunit corresponds to the C-terminal part of ATP-dependent dihydroxykinases and the DhaK subunit corresponds to the N-terminal part.
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.
Sequence similarities	Contains 1 DhaL domain.

Ontologies

Keywords
Biological process	Glycerol metabolism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycerol catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	ADP binding Inferred from direct assay Ref.6. Source: EcoCyc ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glycerone kinase activity Inferred from physical interaction Ref.5. Source: EcoliWiki magnesium ion binding Inferred from direct assay Ref.7. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 210

210

PTS-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL

PRO_0000121530

Regions

Domain

6 – 206

201

DhaL

Nucleotide binding

35 – 41

ADP

Nucleotide binding

79 – 80

ADP

Nucleotide binding

191 – 193

ADP

Sites

Binding site

121

ADP; via carbonyl oxygen

Binding site

178

ADP

Secondary structure

210

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P76014 [UniParc].

Last modified May 30, 2000. Version 3.
Checksum: 91C668A3E792CB5F
Show »

FASTA

210

22,632

        10         20         30         40         50         60 
MSLSRTQIVN WLTRCGDIFS TESEYLTGLD REIGDADHGL NMNRGFSKVV EKLPAIADKD 

        70         80         90        100        110        120 
IGFILKNTGM TLLSSVGGAS GPLFGTFFIR AAQATQARQS LTLEELYQMF RDGADGVISR 

       130        140        150        160        170        180 
GKAEPGDKTM CDVWVPVVES LRQSSEQNLS VPVALEAASS IAESAAQSTI TMQARKGRAS 

       190        200        210 
YLGERSIGHQ DPGATSVMFM MQMLALAAKE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U00096 Genomic DNA. Translation: AAC74283.1.
AP009048 Genomic DNA. Translation: BAA36056.2.

PIR

D64866.

RefSeq

NP_415717.1. NC_000913.2.
YP_489466.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BTD	X-ray	2.60	A	1-210	[»]
3PNL	X-ray	2.20	B	2-210	[»]

ProteinModelPortal

P76014.

SMR

P76014. Positions 2-210.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-11562N.

STRING

511145.b1199.

Proteomic databases

PaxDb

P76014.

PRIDE

P76014.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74283; AAC74283; b1199.
BAA36056; BAA36056; BAA36056.

GeneID

12931768.
945748.

KEGG

ecj:Y75_p1171.
eco:b1199.

PATRIC

32117648. VBIEscCol129921_1246.

Organism-specific databases

EchoBASE

EB3659.

EcoGene

EG13900. dhaL.

Phylogenomic databases

eggNOG

COG2376.

HOGENOM

HOG000226525.

K05879.

OMA

VWIPVIE.

ProtClustDB

PRK10005.

Enzyme and pathway databases

BioCyc

EcoCyc:MONOMER0-1261.
ECOL316407:JW5186-MONOMER.
MetaCyc:MONOMER0-1261.

BRENDA

2.7.1.29. 2026.

UniPathway

UPA00616.

Gene expression databases

Genevestigator

P76014.

Family and domain databases

InterPro

IPR004007. Dak2.
IPR012737. DhaK_L_YcgS.
[Graphical view]

Pfam

PF02734. Dak2. 1 hit.
[Graphical view]

SUPFAM

SSF101473. Dak2. 1 hit.

TIGRFAMs

TIGR02365. dha_L_ycgS. 1 hit.

PROSITE

PS51480. DHAL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P76014.

Entry information

Entry name

DHAL_ECOLI

Accession

Primary (citable) accession number: P76014

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	May 1, 2013
This is version 102 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents