B3DYW2 · MURA_METI4
- ProteinUDP-N-acetylglucosamine 1-carboxyvinyltransferase
- GenemurA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids421 (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 | 91 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 115 | Proton donor | ||||
Sequence: C | ||||||
Binding site | 120-124 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: RPIDL | ||||||
Binding site | 306 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 328 | 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
- Strain
- Taxonomic lineageBacteria > Verrucomicrobiota > Methylacidiphilae > Methylacidiphilales > Methylacidiphilaceae > Methylacidiphilum (ex Ratnadevi et al. 2023)
Accessions
- Primary accessionB3DYW2
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000094700 | 1-421 | UDP-N-acetylglucosamine 1-carboxyvinyltransferase | |||
Sequence: MEKFIIKGGNPLEGKITISGSKNSALPILAATLLTPEECVIHRVPNLSDIRYMLEILKFLGAQVHYEKGTVRIKSKIVHSTAPYDLVRKMRASICILGPLIARCGQARVSLPGGCVIGDRPIDLHITGLQKLGADIEIIKGDVVAHGGILRGTSINLKGKYGSTVLGTDNVMMAACQAEGTTIIEGAACEPEVEDLAHFLSSMGAKISGMGTQQLIIEGVKELHGCEYTIITDRIEAGTFAVAAAMTKGNLLLEHAPVEHMGSVLEKLKDCGASIEIESQGIRVSRSGPLRAFEIVTAAYPGFPTDMQAQFCAMATVAEGTSKIVENIFPNRFMHISELKRLGAMIELSQNQALIHGTERLSGAPVMASDLRASAALVLAGLVAENTTEVHRVYHIDRGYEKIDEKLSSVGANITRVYSKI | ||||||
Modified residue | 115 | 2-(S-cysteinyl)pyruvic acid O-phosphothioketal | ||||
Sequence: C |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length421
- Mass (Da)45,138
- Last updated2008-07-22 v1
- ChecksumBC4D16ACFFA8ED4F
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000975 EMBL· GenBank· DDBJ | ACD82484.1 EMBL· GenBank· DDBJ | Genomic DNA |