A0A927BJ83 · A0A927BJ83_STRGL
- ProteinUDP-N-acetylglucosamine 1-carboxyvinyltransferase
- GenemurA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids446 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Catalytic activity
- phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Pathway
Cell wall biogenesis; peptidoglycan biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 26-27 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: KN | ||||||
Binding site | 100 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 124 | Proton donor | ||||
Sequence: C | ||||||
Binding site | 314 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 336 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: V |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity | |
Biological Process | cell division | |
Biological Process | cell wall organization | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | regulation of cell shape | |
Biological Process | UDP-N-acetylgalactosamine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUDP-N-acetylglucosamine 1-carboxyvinyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionA0A927BJ83
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 124 | 2-(S-cysteinyl)pyruvic acid O-phosphothioketal | ||||
Sequence: C |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-431 | Enolpyruvate transferase | ||||
Sequence: HGGTPLEGEIRVRGAKNLVPKAMVAALLGSGPSRLRNVPDIRDVRVVRGLLQLHGVTVRPGDEPGELILDPSHVESANVADIDAHAGSSRIPILFCGPLLHRLGHAFIPGLGGCDIGGRPIDFHFEVLRQFGATIEKRADGQYLEAPQRLRGTKIRLPYPSVGSTEQVLLTAVLAEGVTELSNAAVEPEIEDLICVLQKMGAIISMDTDRTIRITGVDRLDGYTHRALPDRLEAASWASAALATEGNIYVRGAQQRSMMTFLNTYRKVGGAFEIDDEGIRFWHPGGALNAIALETDVHPGFQTDWQQPLVVALTQAAGLSIVHETVYESRLGFTSALNQMGAHIQLYRECLGGSDCRFGQRNFLHSAVVSGPTKLQGADLVIPDLRGGFSYLIAALAAQGTSRVHGIDLINRGYENFMEKL |
Sequence similarities
Belongs to the EPSP synthase family. MurA subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length446
- Mass (Da)48,050
- Last updated2023-02-22 v1
- Checksum61B47EA9C8AF8A66