2.3.1.191: UDP-3-O-(3-hydroxyacyl)glucosamine N-acyltransferase

This is an abbreviated version!
For detailed information about UDP-3-O-(3-hydroxyacyl)glucosamine N-acyltransferase, go to the full flat file.

Reaction

Synonyms

acyl-ACP:UDP-3-O-(3-hydroxyacyl)-GlcN N-acyltransferase, acyltransferase LpxD, CtLpxD, EcLpxD, firA, La0512, LpxD, LpxD1, Lpxd2, PA3646, UDP-3-O-(R-3-hydroxyacyl)-glucosamine acyltransferase, UDP-3-O-acyl-glucosamine N-acyltransferase

ECTree

     2 Transferases

         2.3 Acyltransferases

             2.3.1 Transferring groups other than aminoacyl groups

                2.3.1.191 UDP-3-O-(3-hydroxyacyl)glucosamine N-acyltransferase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
1	Activating Compound
23563	AA Sequence
1	Application
14	Cloned(Commentary)
6	Crystallization (Commentary)
22	General Information
2	IC50 Value
11	Inhibitors
11	kcat/KM [mM/s]
7	Ki Value [mM]
25	KM Value [mM]
2	Localization
3	Molecular Weight [Da]
9	Natural Substrates/ Products (Substrates)
33	Organism
11	Pathway
45	PDB ID
2	pH Optimum
16	Protein Variants
7	Purification (Commentary)
1	Reaction
29	Reference
2	Source Tissue
2	Specific Activity [micromol/min/mg]
21	Substrates and Products (Substrate)
4	Subunits
32	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
24	Turnover Number [1/s]

Subunits

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Subunits on EC 2.3.1.191 - UDP-3-O-(3-hydroxyacyl)glucosamine N-acyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide show all columns Go to Subunit Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

homotrimer

3 entries

additional information

Pseudomonas aeruginosa

Q9HXY6

the LpxD domain architecture is consisting of an N-terminal domain, amino acids 2-95, a left-handed beta-helix central domain containing many short parallel beta-sheet segments wrappingthrough consecutive triangular sections, amino acids 101-305, and a C-terminal helix, amino acids 312-340

718513

homotrimer

Chlamydia trachomatis

P0CD76

each subunit of which is constructed from a novel combination of an N-terminal uridine binding domain, a core lipid-binding domain, and a C-terminal helical extension. Highly conserved residues dominate nucleotide binding. Phe43 and Tyr49 form pi-stacking interactions with uracil, and Asn46 and His284 form hydrogen bonds with the phosphate groups

700935

homotrimer

Escherichia coli

-

3 * 35880, electrospray-ionization/time-of-flight mass spectrometry

696264

homotrimer

Escherichia coli

-

3 * 35881, calculated from sequence

696264