A0A2Z5E6E6 · A0A2Z5E6E6_9SPHN
- ProteinUDP-N-acetylglucosamine 1-carboxyvinyltransferase
- GenemurA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids427 (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 | 22-23 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: KN | ||||||
Binding site | 99 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 123 | Proton donor | ||||
Sequence: C | ||||||
Binding site | 128-132 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: RPIDL | ||||||
Binding site | 313 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 335 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: I |
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 > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Novosphingobium
Accessions
- Primary accessionA0A2Z5E6E6
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 123 | 2-(S-cysteinyl)pyruvic acid O-phosphothioketal | ||||
Sequence: C |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 7-414 | Enolpyruvate transferase | ||||
Sequence: EGGKRLSGTIPVSGAKNAALTLLPCALLTEEPLTLRNLPRLADIDGFQHLMNQFGISTAIAGSRPEDFGRVMTLQATRITSSVAPYDLVRKMRASILVLGPMLARMGEATVSLPGGCAIGNRPIDLHLKVIEALGATIEMAAGYVRAIAPDGGLPGGRYSFPVVSVGATENALMTAVLCNGKSTLHNAAREPEIVDLCNLLVAMGAQIEGIGTSDITIHGVPRLHGATYMVMPDRIEAGSYACAAAITGGEVLLKGARIEDMEATVQALRDAGVHVEPKADGIYVAAEGKLKPVTLSTAPYPGFATDMQAQLMALLCRAEGSSVLTETIFENRYMHVPELNRMGARIETKGRTAIVHGVDKLAGADVMATDLRASMSLVIAGLAAEGQTQVHRLYHLDRGYERLEEKL |
Sequence similarities
Belongs to the EPSP synthase family. MurA subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length427
- Mass (Da)45,139
- Last updated2018-10-10 v1
- ChecksumDC471F607D3BAE01
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP030352 EMBL· GenBank· DDBJ | AXB75219.1 EMBL· GenBank· DDBJ | Genomic DNA |