Q4QLK7 · MURA_HAEI8
- ProteinUDP-N-acetylglucosamine 1-carboxyvinyltransferase
- GenemurA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids424 (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 | 93 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 117 | Proton donor | ||||
Sequence: C | ||||||
Binding site | 122-126 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: RPVDL | ||||||
Binding site | 162-165 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: KVSV | ||||||
Binding site | 307 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 329 | 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 > Pseudomonadota > Gammaproteobacteria > Pasteurellales > Pasteurellaceae > Haemophilus
Accessions
- Primary accessionQ4QLK7
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000231211 | 1-424 | UDP-N-acetylglucosamine 1-carboxyvinyltransferase | |||
Sequence: MDKFRVYGQSRLSGSVNISGAKNAALPILFAAILATEPVKLTNVPELKDIETTLNILRQLGVIANRDETGAVLLDASNINHFTAPYELVKTMRASIWALAPLVARFHQAQVSLPGGCSIGARPVDLHISGLEKLGADIVLEEGYVKAQVSDRLVGTRIVIEKVSVGATLSIMMAATLAKGTTVIENAAREPEIVDTADFLNKMGAKITGAGSDHITTEGVERLTGCEHSIVPDRIETGTFLIAAAISGGRVVCQNTKADTLDAVIDKLREAGAQVDVTENSITLDMLGNRPKAVNIRTAPHPGFPTDMQAQFTLLNMVAEGTSIITETIFENRFMHIPELIRMGGKAEIEGNTAVCHGVEQLSGTEVIATDLRASISLVLAGCIATGETIVDRIYHIDRGYEHIEDKLRALGAKIERFSRSDEA | ||||||
Modified residue | 117 | 2-(S-cysteinyl)pyruvic acid O-phosphothioketal | ||||
Sequence: C |
Interaction
Chemistry
Structure
Sequence
- Sequence statusComplete
- Length424
- Mass (Da)45,442
- Last updated2005-07-19 v1
- Checksum0C0D96D346482566
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000057 EMBL· GenBank· DDBJ | AAX88090.1 EMBL· GenBank· DDBJ | Genomic DNA |