O25511 · PSEB_HELPY
- ProteinUDP-N-acetylglucosamine 4,6-dehydratase (inverting)
- GenepseB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids333 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the first step in the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is used to modify flagellin. Has both C6 dehydratase and C5 epimerase activities that result in the production of both UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose and UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose.
Catalytic activity
- UDP-N-acetyl-alpha-D-glucosamine = UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
159 μM | UDP-GlcNAc |
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 19-22 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: TGSF | ||||||
Binding site | 43-48 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SRDELK | ||||||
Binding site | 67-68 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: DV | ||||||
Binding site | 87 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 91 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 91 | substrate | ||||
Sequence: K | ||||||
Binding site | 129-130 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: LS | ||||||
Active site | 133 | |||||
Sequence: K | ||||||
Binding site | 141 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 145 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 173 | substrate | ||||
Sequence: N | ||||||
Binding site | 174-178 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: VVGSR | ||||||
Binding site | 181 | substrate | ||||
Sequence: V | ||||||
Binding site | 199 | substrate | ||||
Sequence: T | ||||||
Binding site | 258 | substrate | ||||
Sequence: R | ||||||
Binding site | 261 | substrate | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | lyase activity | |
Molecular Function | nucleotide binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUDP-N-acetylglucosamine 4,6-dehydratase (inverting)
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Campylobacterota > Epsilonproteobacteria > Campylobacterales > Helicobacteraceae > Helicobacter
Accessions
- Primary accessionO25511
Proteomes
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 133 | Loss of activity. | ||||
Sequence: K → A or E |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000418954 | 1-333 | UDP-N-acetylglucosamine 4,6-dehydratase (inverting) | |||
Sequence: MPNHQNMLDNQTILITGGTGSFGKCFVRKVLDTTNAKKIIVYSRDELKQSEMAMEFNDPRMRFFIGDVRDLERLNYALEGVDICIHAAALKHVPIAEYNPLECIKTNIMGASNVINACLKNAISQVIALSTDKAANPINLYGATKLCSDKLFVSANNFKGSSQTQFSVVRYGNVVGSRGSVVPFFKKLVQNKASEIPITDIRMTRFWITLDEGVSFVLKSLKRMHGGEIFVPKIPSMKMTDLAKALAPNTPTKIIGIRPGEKLHEVMIPKDESHLALEFEDFFIIQPTISFQTPKDYTLTKLHEKGQKVAPDFEYSSHNNNQWLEPDDLLKLL |
Proteomic databases
Structure
Sequence
- Sequence statusComplete
- Length333
- Mass (Da)37,354
- Last updated1998-01-01 v1
- Checksum8EF0A39F0FBF0516
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE000511 EMBL· GenBank· DDBJ | AAD07887.1 EMBL· GenBank· DDBJ | Genomic DNA |