PTS-dependent dihydroxyacetone kinase, dihydroxyacetone-binding subunit dhaK

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P76015 (DHAK_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 98. History...

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

Documents (4) |

Third-party data

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

Names and origin

Protein names

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

Gene names

Name:	dhaK
Synonyms:	ycgT
Ordered Locus Names:	b1200, JW5187

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	356 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for phosphorylating dihydroxyacetone. Binds covalently dihydroxyacetone in hemiaminal linkage. Acts also as a corepressor of dhaR by binding to its sensor domain, in the absence of dihydroxyacetone.
Pathway	Polyol metabolism; glycerol degradation.
Subunit structure	Homodimer. The dihydroxyacetone kinase complex is composed of a homodimer of dhaM, a homodimer of dhaK and the subunit dhaL. Ref.4 Ref.5
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.
Sequence similarities	Contains 1 DhaK domain.
Biophysicochemical properties	Kinetic parameters: K_M=6 µM for dihydroxyacetone Ref.5

Ontologies

Keywords
Biological process	Glycerol metabolism
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glycerol metabolic process Inferred from electronic annotation. Source: UniProtKB-KW monosaccharide catabolic process Inferred from mutant phenotype. Source: EcoCyc
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	glycerone kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
guaC	P60560	1	EBI-544485,EBI-544491
yhiH	P37624	1	EBI-544485,EBI-544500

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 356

356

PTS-dependent dihydroxyacetone kinase, dihydroxyacetone-binding subunit dhaK

PRO_0000121529

Regions

Domain

7 – 352

346

DhaK

Region

53 – 56

Substrate binding

Sites

Active site

218

Tele-hemiaminal-histidine intermediate Ref.4 Ref.5

Binding site

104

Substrate

Binding site

109

Substrate

Experimental info

Mutagenesis

218

H → A or K: Loss of kinase activity. Ref.4

Secondary structure

356

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P76015 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: 510D73BE9685395F
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FASTA

356

38,215

        10         20         30         40         50         60 
MKKLINDVQD VLDEQLAGLA KAHPSLTLHQ DPVYVTRADA PVAGKVALLS GGGSGHEPMH 

        70         80         90        100        110        120 
CGYIGQGMLS GACPGEIFTS PTPDKIFECA MQVDGGEGVL LIIKNYTGDI LNFETATELL 

       130        140        150        160        170        180 
HDSGVKVTTV VIDDDVAVKD SLYTAGRRGV ANTVLIEKLV GAAAERGDSL DACAELGRKL 

       190        200        210        220        230        240 
NNQGHSIGIA LGACTVPAAG KPSFTLADNE MEFGVGIHGE PGIDRRPFSS LDQTVDEMFD 

       250        260        270        280        290        300 
TLLVNGSYHR TLRFWDYQQG SWQEEQQTKQ PLQSGDRVIA LVNNLGATPL SELYGVYNRL 

       310        320        330        340        350 
TTRCQQAGLT IERNLIGAYC TSLDMTGFSI TLLKVDDETL ALWDAPVHTP ALNWGK

« 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: 8905232] [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: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"A mechanism of covalent substrate binding in the X-ray structure of subunit K of the Escherichia coli dihydroxyacetone kinase." Siebold C., Garcia-Alles L.F., Erni B., Baumann U. Proc. Natl. Acad. Sci. U.S.A. 100:8188-8192(2003) [PubMed: 12813127] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH DIHYDROXYACETONE, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF HIS-218.
[5]	"Phosphoenolpyruvate- and ATP-dependent dihydroxyacetone kinases: covalent substrate-binding and kinetic mechanism." Garcia-Alles L.F., Siebold C., Luethi Nyffeler T., Fluekiger-Bruehwiler K., Schneider P., Buergi H.-B., Baumann U., Erni B. Biochemistry 43:13037-13045(2004) [PubMed: 15476397] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH DIHYDROXYACETONE PHOSPHATE, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U00096 Genomic DNA. Translation: AAC74284.2.
AP009048 Genomic DNA. Translation: BAA36057.2.

PIR

E64866.

RefSeq

NP_415718.6. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OI2	X-ray	1.75	A/B	1-356	[»]
1OI3	X-ray	2.00	A/B	1-356	[»]
1UOD	X-ray	1.90	A/B	1-356	[»]
1UOE	X-ray	2.00	A/B	1-356	[»]
3PNK	X-ray	2.21	A/B	2-356	[»]
3PNL	X-ray	2.20	A	2-356	[»]
3PNM	X-ray	2.55	A/B/C/D	2-356	[»]
3PNO	X-ray	1.97	A/B/C/D	2-356	[»]
3PNQ	X-ray	2.20	A/B/C/D	2-356	[»]

ProteinModelPortal

P76015.

SMR

P76015. Positions 2-356.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-11563N.

IntAct

P76015. 6 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001030; EBESCP00000001030; EBESCG00000000849.
EBESCT00000014559; EBESCP00000013850; EBESCG00000013620.

GeneID

945747.

GenomeReviews

Gene locus JW5187 in contig AP009048_GR.
Gene locus b1200 in contig U00096_GR.

KEGG

ecj:JW5187.
eco:b1200.

PATRIC

32117650. VBIEscCol129921_1247.

Organism-specific databases

EchoBASE

EB3660.

EcoGene

EG13901. dhaK.

Phylogenomic databases

eggNOG

COG2376.

GeneTree

EBGT00050000009462.

HOGENOM

HBG473357.

OMA

TSLEMQG.

PhylomeDB

P76015.

ProtClustDB

PRK11468.

Enzyme and pathway databases

BioCyc

EcoCyc:G6627-MONOMER.
MetaCyc:G6627-MONOMER.

BRENDA

2.7.1.29. 2026.

Gene expression databases

Genevestigator

P76015.

Family and domain databases

InterPro

IPR004006. Dak1.
IPR012736. DhaK_1.
[Graphical view]

K05878.

Pfam

PF02733. Dak1. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02363. DhaK1. 1 hit.

PROSITE

PS51481. DHAK. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DHAK_ECOLI

Accession

Primary (citable) accession number: P76015

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 13, 2007
Last modified:	January 25, 2012
This is version 98 of the entry and version 2 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents