2.3.1.203: UDP-N-acetylbacillosamine N-acetyltransferase

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For detailed information about UDP-N-acetylbacillosamine N-acetyltransferase, go to the full flat file.

Reaction

Synonyms

ABAYE3807, Cj1123c, NGO_0085, PglD, WeeI

ECTree

     2 Transferases

         2.3 Acyltransferases

             2.3.1 Transferring groups other than aminoacyl groups

                2.3.1.203 UDP-N-acetylbacillosamine N-acetyltransferase

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Results	in table
292	AA Sequence
2	Application
4	Cloned(Commentary)
1	Cofactor
3	Crystallization (Commentary)
2	General Information
39	IC50 Value
39	Inhibitors
10	kcat/KM [mM/s]
10	KM Value [mM]
4	Localization
3	Molecular Weight [Da]
40	Organism
3	Pathway
3	PDB ID
14	Protein Variants
4	Purification (Commentary)
1	Reaction
13	Reference
9	Substrates and Products (Substrate)
3	Subunits
18	Synonyms
1	Systematic Name
10	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.3.1.203 - UDP-N-acetylbacillosamine N-acetyltransferase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

compared to isoforms PglD and PglB, WeeI contains an additional loop (Gln174-Pro180) that forms the substrate binding pocket near the pyranose moiety. Residue Gln174 seems to be critical for catalysis. When aligned to the PglD UDP-4-amino structure, this position is analogous to Asn162 that interacts with the carbonyl oxygen of the pyranose C2-acetyl group. In the WeeI apo-structure, Gln174 is within 5 A of the catalytic base His138 and 3.6 A of the AcCoA thioester

Acinetobacter baumannii

B0V6J7

736434

apoenzyme or in complex with CoA, hanging drop vapor diffusion method, using 0.1 M sodium acetate (pH 4.5) and 1.9 M ammonium sulfate, at 30°C

Campylobacter jejuni

Q0P9D1

718849

apo-crystal structures of the acetyltransferase domain ATD and in complex with AcCoA. The N-terminal section (Asn199-Leu285) comprises a binding pocket for the UDP-4-amino sugar substrate through a beta-alpha-beta-alpha-beta Rossman fold motif. The C-terminus (Pro286-Leu403) is composed of a left-handed beta-helix motif that, in conjunction with an adjacent PglB-ATD protomer in the trimeric state, forms an extended cleft that is utilized for AcCoA binding

Neisseria gonorrhoeae

Q5FAE1

736434