ECOLI:DHAL

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	dhaL (synonyms: ycgS)
Protein Name(s)	PTS-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL
External Links
UniProt	P76014
EMBL	U00096 AP009048
PIR	D64866
RefSeq	NP_415717.1 YP_489466.1
PDB	2BTD 3PNL 4LRZ
PDBsum	2BTD 3PNL 4LRZ
ProteinModelPortal	P76014
SMR	P76014
DIP	DIP-11562N
STRING	511145.b1199
MoonProt	P76014
PaxDb	P76014
PRIDE	P76014
EnsemblBacteria	AAC74283 BAA36056
GeneID	12931768 945748
KEGG	ecj:Y75_p1171 eco:b1199
PATRIC	32117648
EchoBASE	EB3659
EcoGene	EG13900
eggNOG	COG2376
HOGENOM	HOG000226525
InParanoid	P76014
KO	K05879
OMA	SAFMGMA
OrthoDB	EOG65J57G
PhylomeDB	P76014
BioCyc	EcoCyc:MONOMER0-1261 ECOL316407:JW5186-MONOMER MetaCyc:MONOMER0-1261 RETL1328306-WGS:GSTH-4273-MONOMER
BRENDA	2.7.1.29
UniPathway	UPA00616
EvolutionaryTrace	P76014
PRO	PR:P76014
Proteomes	UP000000318 UP000000625
Genevestigator	P76014
GO	GO:0043531 GO:0005524 GO:0004371 GO:0000287 GO:0019563
InterPro	IPR012737 IPR004007
Pfam	PF02734
SUPFAM	SSF101473
TIGRFAMs	TIGR02365
PROSITE	PS51480

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
Contributes to	GO:0016740	transferase activity	PMID:11350937^[1]	ECO:0000314			F	See Fig. 4C.	complete
enables	GO:0005524	ATP binding	PMID:24440518^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:24440518^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0047324	phosphoenolpyruvate-glycerone phosphotransferase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q92EU3	F	Seeded From UniProt	complete
enables	GO:0043531	ADP binding	PMID:15753087^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:15911532^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:16647083^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004371	glycerone kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004007 InterPro:IPR036117	F	Seeded From UniProt	complete
involved_in	GO:0006071	glycerol metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004007 InterPro:IPR036117	P	Seeded From UniProt	complete
enables	GO:0016772	transferase activity, transferring phosphorus-containing groups	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012737	F	Seeded From UniProt	complete
enables	GO:0047324	phosphoenolpyruvate-glycerone phosphotransferase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.1.121	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	F	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
involved_in	GO:0006071	glycerol metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0319	P	Seeded From UniProt	complete
involved_in	GO:0016310	phosphorylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	P	Seeded From UniProt	complete
involved_in	GO:0019563	glycerol catabolic process	GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniPathway:UPA00616	P	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Gutknecht, R et al. (2001) The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor. EMBO J. 20 2480-6 PubMed GONUTS page
↑ ^2.0 ^2.1 Shi, R et al. (2014) Coiled-coil helix rotation selects repressing or activating state of transcriptional regulator DhaR. Structure 22 478-87 PubMed GONUTS page
↑ Bächler, C et al. (2005) From ATP as substrate to ADP as coenzyme: functional evolution of the nucleotide binding subunit of dihydroxyacetone kinases. J. Biol. Chem. 280 18321-5 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
↑ Oberholzer, AE et al. (2006) Crystal structure of the nucleotide-binding subunit DhaL of the Escherichia coli dihydroxyacetone kinase. J. Mol. Biol. 359 539-45 PubMed GONUTS page

[PMID:11350937-1] Gutknecht, R et al. (2001) The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor. EMBO J. 20 2480-6 PubMed GONUTS page

[PMID:24440518-2] 2.0 ^2.1 Shi, R et al. (2014) Coiled-coil helix rotation selects repressing or activating state of transcriptional regulator DhaR. Structure 22 478-87 PubMed GONUTS page

[PMID:15753087-3] Bächler, C et al. (2005) From ATP as substrate to ADP as coenzyme: functional evolution of the nucleotide binding subunit of dihydroxyacetone kinases. J. Biol. Chem. 280 18321-5 PubMed GONUTS page

[PMID:18304323-4] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:15911532-5] Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

[PMID:16647083-6] Oberholzer, AE et al. (2006) Crystal structure of the nucleotide-binding subunit DhaL of the Escherichia coli dihydroxyacetone kinase. J. Mol. Biol. 359 539-45 PubMed GONUTS page

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ECOLI:DHAL

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