Q5LZI4 · MURA1_STRT1
- ProteinUDP-N-acetylglucosamine 1-carboxyvinyltransferase 1
- GenemurA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids423 (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 | 23-24 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: KN | ||||||
Binding site | 96 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 120 | Proton donor | ||||
Sequence: C | ||||||
Binding site | 125-129 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: RPIDL | ||||||
Binding site | 309 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 331 | 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 1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus
Accessions
- Primary accessionQ5LZI4
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000231284 | 1-423 | UDP-N-acetylglucosamine 1-carboxyvinyltransferase 1 | |||
Sequence: MDKIIVKGGNTRLSGEVVIEGAKNAVLPLLAATILASEGQTTLTNVPILSDVYTMNNVVRGLDIAVDFDEENNTVVVDASGEILDQAPYEYVSKMRASIVVLGPILARNGHAKVSMPGGCTIGSRPIDLHLKGLEAMGAKITQVGGDITATAEKLKGATIYMDFPSVGATQNLMMAATLADGVTTIENAAREPEIVDLAILLNEMGANVKGAGTEKLVIKGVKSLHGTQHAVIQDRIEAGTFMVAAAMTSGNVLIKDAIWEHNRPLISKLLEMGVDVKEEDRGIRVKSDVSKLKPVAVKTLPHPGFPTDMQAQFTALMAVVKGKSSISETVFENRFQHLEEMRRMGLHSEILRDTAMIHGGLPLQGARVMSTDLRASAALILTGMVAEGTTTVGKLTHLDRGYYKFHEKLAKLGAQISRVSEA | ||||||
Modified residue | 120 | 2-(S-cysteinyl)pyruvic acid O-phosphothioketal | ||||
Sequence: C |
Structure
Sequence
- Sequence statusComplete
- Length423
- Mass (Da)45,182
- Last updated2006-04-04 v2
- Checksum51C09E3FEF6F586A
Sequence caution
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000024 EMBL· GenBank· DDBJ | AAV62715.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation |