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87  structures 2236  species 1  interaction 2412  sequences 8  architectures

Family: DAGK_prokar (PF01219)

Summary: Prokaryotic diacylglycerol kinase

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This is the Wikipedia entry entitled "Diacylglycerol kinase". More...

Diacylglycerol kinase Edit Wikipedia article

Diacylglycerol kinase
Soluble diacylglycerol kinase DgkB from Staphylococcus aureus.png
DgkB, soluble DAGK from Staphylococcus aureus. α-helices in red, β-strands in yellow, coils in green.
Identifiers
EC number 2.7.1.107
CAS number 60382-71-0
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Prokaryotic diacylglycerol kinase
Identifiers
Symbol DAGK_prokar
Pfam PF01219
InterPro IPR000829
PROSITE PDOC00820
OPM superfamily 217
OPM protein 2kdc
Diacylglycerol kinase catalytic domain
Identifiers
Symbol DAGK_cat
Pfam PF00781
Pfam clan CL0240
InterPro IPR001206
SMART DAGKc
Diacylglycerol kinase accessory domain
Identifiers
Symbol DAGK_acc
Pfam PF00609
InterPro IPR000756
SMART DAGKa

Diacylglycerol kinase (DGK or DAGK) is a family of enzymes that catalyzes the conversion of diacylglycerol (DAG) to phosphatidic acid (PA) utilizing ATP as a source of the phosphate. In non-stimulated cells, DGK activity is low allowing DAG to be used for glycerophospholipid biosynthesis but on receptor activation of the phosphoinositide pathway, DGK activity increases driving the conversion of DAG to PA. As both lipids are thought to function as bioactive lipid signaling molecules with distinct cellular targets, DGK therefore occupies an important position, effectively serving as a switch by terminating the signalling of one lipid while simultaneously activating signalling by another.[1]

In bacteria, DGK is very small (13 to 15 kD) membrane protein which seems to contain three transmembrane domains.[2] The best conserved region is a stretch of 12 residues which are located in a cytoplasmic loop between the second and third transmembrane domains. Some Gram-positive bacteria also encode a soluble diacylglycerol kinase capable of reintroducing DAG into the phospholipid biosynthesis pathway. DAG accumulates in Gram-positive bacteria as a result of the transfer of glycerol-1-phosphate moieties from phosphatidylglycerol to lipotechoic acid.[3]

Mammalian DGK Isoforms

Currently, nine members of the DGK family have been cloned and identified. Although all family members have conserved catalytic domains and two cysteine rich domains, they are further classified into five groups according to the presence of additional functional domains and substrate specificity.[4] These are as follows:

  • Type 1 - DGK-α, DGK-β, DGK-γ - contain EF-hand motifs and a recoverin homology domain
  • Type 2 - DGK-δ, DGK-η - contain a pleckstrin homology domain
  • Type 3 - DGK-ε - has specificity for arachidonate-containing DAG
  • Type 4 - DGK-ζ, DGK-ι - contain a MARCKS homology domain, ankyrin repeats, a C-terminal nuclear localisation signal, and a PDZ-binding motif.
  • Type 5 - DGK-θ - contains a third cysteine-rich domain, a pleckstrin homology domain and a proline rich region

References

  1. ^ Merida I, Avila-Flores A, Merino E (2008). "Diacylglycerol kinases: at the hub of cell signalling.". Biochem. J. 409 (1): 1–18. doi:10.1042/BJ20071040. PMID 18062770. 
  2. ^ Smith RL, O'Toole JF, Maguire ME, Sanders CR (September 1994). "Membrane topology of Escherichia coli diacylglycerol kinase". J. Bacteriol. 176 (17): 5459–65. PMC 196734Freely accessible. PMID 8071224. 
  3. ^ Miller DJ, Jerga A, Rock CO, White SW (July 2008). "Analysis of the Staphylococcus aureus DgkB structure reveals a common catalytic mechanism for the soluble diacylglycol kinases". Structure. 16 (7): 1036–46. doi:10.1016/j.str.2008.03.019. PMC 2847398Freely accessible. PMID 18611377. 
  4. ^ Van Blitterswijk, WJ; Houssa, B (2000). "Properties and functions of diacylglycerol kinases.". Cellular Signaling. 12 (9–10): 595–605. doi:10.1016/s0898-6568(00)00113-3. PMID 11080611. 

External links

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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Prokaryotic diacylglycerol kinase Provide feedback

No Pfam abstract.

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000829

Prokaryotic diacylglycerol kinase (DAGK) and undecaprenol kinase (UDPK) constitute a family of multispan membrane enzymes that are very small, lack relationships to any other family of proteins and exhibit an unusual structure. Escherichia coli DAGK plays an important role in recycling diacylglycerol produced as a by-product of biosynthesis of molecules located in the periplasmic space. UDPK seems to play an analogous role in Gram-positive bacteria, where it is essential for biofilm formation by the oral pathogen Streptococcus mutans [PUBMED:22224599].

Diacylglycerol kinase (EC) (DAGK) is an enzyme that catalyses the formation of phosphatidic acid from diacylglycerol and ATP, an important step in phospholipid biosynthesis. In bacteria DAGK is very small (13 to 15 kD) membrane protein which seems to contain three transmembrane domains [PUBMED:8071224].

Gene Ontology

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Domain organisation

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(606)
Full
(2412)
Representative proteomes UniProt
(8059)
NCBI
(10662)
Meta
(401)
RP15
(452)
RP35
(1423)
RP55
(2481)
RP75
(4071)
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Key: ✓ available, x not generated, not available.

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  Seed
(606)
Full
(2412)
Representative proteomes UniProt
(8059)
NCBI
(10662)
Meta
(401)
RP15
(452)
RP35
(1423)
RP55
(2481)
RP75
(4071)
Alignment:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(606)
Full
(2412)
Representative proteomes UniProt
(8059)
NCBI
(10662)
Meta
(401)
RP15
(452)
RP35
(1423)
RP55
(2481)
RP75
(4071)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

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Curation View help on the curation process

Seed source: Prosite
Previous IDs: none
Type: Family
Author: Finn RD, Bateman A
Number in seed: 606
Number in full: 2412
Average length of the domain: 100.90 aa
Average identity of full alignment: 33 %
Average coverage of the sequence by the domain: 73.99 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.3 22.3
Trusted cut-off 25.2 25.0
Noise cut-off 22.2 22.2
Model length: 102
Family (HMM) version: 18
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

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Interactions

There is 1 interaction for this family. More...

DAGK_prokar

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the DAGK_prokar domain has been found. There are 87 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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