Reviewed, UniProtKB/Swiss-Prot P76015 (DHAK_ECOLI)

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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	356 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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
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 DAK1 (dihydroxyacetone kinase subunit 1) domain.

Ontologies

Keywords
Biological process	Glycerol metabolism
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	glycerol metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	glycerone kinase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
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

16 – 356

341

DAK1

Sites

Active site

218

1

Tele-hemiaminal-histidine intermediate

Binding site

56

1

Substrate

Binding site

109

1

Substrate

Experimental info

Mutagenesis

218

1

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

Secondary structure

1

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356

Helix Strand Turn

Details...

Helix

11 – 22

12

Beta strand

26 – 29

4

Turn

30 – 33

4

Beta strand

34 – 37

4

Beta strand

47 – 56

10

Turn

57 – 60

4

Helix

61 – 63

3

Beta strand

64 – 66

3

Beta strand

68 – 77

10

Helix

83 – 93

11

Beta strand

99 – 106

8

Helix

107 – 122

16

Beta strand

127 – 132

6

Beta strand

145 – 147

3

Helix

152 – 166

15

Helix

170 – 181

12

Beta strand

184 – 192

9

Beta strand

210 – 213

4

Beta strand

223 – 227

5

Helix

231 – 244

14

Beta strand

248 – 256

9

Turn

257 – 260

4

Beta strand

261 – 269

9

Beta strand

277 – 284

8

Helix

290 – 307

18

Beta strand

310 – 317

8

Beta strand

325 – 335

11

Helix

337 – 344

8

Beta strand

347 – 351

5

Sequences

	Sequence		Length	Mass (Da)
	P76015-1 [UniParc]. Last modified November 13, 2007. Version 2. Checksum: 510D73BE9685395F	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

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. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., 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: SUBUNIT, MUTAGENESIS OF HIS-218, X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH DIHYDROXYACETONE.
[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.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

PIR

E64866.

RefSeq

AP_001825.1.
NP_415718.6.

3D structure databases

PDBPDBe

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	[»]

SMR

P76015. Positions 20-366.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:11563N.

IntAct

P76015. 4 interactions.

Genome annotation databases

GeneID

945747.

GenomeReviews

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

KEGG

ecj:JW5187.
eco:b1200.

Organism-specific databases

EchoBASE

EB3660.

EcoGene

EG13901. dhaK.

CMR

Search...

Phylogenomic databases

HOGENOM

P76015.

OMA

P76015. HGEPGTH.

Enzyme and pathway databases

BioCyc

EcoCyc:G6627-MON.
MetaCyc:G6627-MON.

BRENDA

2.7.1.29. 246.

Family and domain databases

InterPro

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

Pfam

PF02733. Dak1. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02363. dhaK1. 1 hit.

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:	June 16, 2009
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)