A0A0G1RQ58 · A0A0G1RQ58_9BACT
- ProteinUDP-N-acetylglucosamine 1-carboxyvinyltransferase
- GenemurA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids981 (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 = UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + phosphate
Pathway
Cell wall biogenesis; peptidoglycan biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 580-581 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: KN | ||||||
Binding site | 650 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 674 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 864 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 886 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: M |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | membrane | |
Molecular Function | penicillin binding | |
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
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUDP-N-acetylglucosamine 1-carboxyvinyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageBacteria > Candidatus Woesebacteria
Accessions
- Primary accessionA0A0G1RQ58
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 49-207 | Penicillin-binding protein dimerisation | ||||
Sequence: SAPRGNILAKDGTWLAARGEAFRVYAELPRLTDSAKKIAEALAPFFVPDAGDRGSLLVEIDRLEGLLAKKEVVWVALKEKVPAPVKQNIEALRFSGIGFEAQEERVYPEASSSAHLLGFVGKNEEGGDVGYFGLEGYYNLSLSGKPGFEALEKDAAGVP | ||||||
Domain | 252-551 | Penicillin-binding protein transpeptidase | ||||
Sequence: GTGIIMNPKTGAILAMSSYPAYDPKTYFDFGDSFFKNPAVSDSFEPGSVFKVLVMAAALDAKAVEPDTKCDICAGPLKVDKYTIETWNRQYRPDSTMVDVIVHSDNVGMTFVGSRLGAETLYDYLERFGIGGLTGIDLQGEASPRLRERGTWNIVDLATASFGQGVAVTPIQMIKAVSAIANGGRVVRPQVVDKLLGESWEEKIKPEIGERVISEETAKEITAMMVLAAKEGEAKWTHLKGFSVAGKTGTAQIPISGHYDDEKTIASFIGFAPSDKPKFIMLVTLREPQTSPWASETAAT | ||||||
Domain | 565-965 | Enolpyruvate transferase | ||||
Sequence: SGGKKLEGKVKVAGSKNSALALVSGALLADSPVTLTNVPEIRDIEVMTQLIEKLGGRVEKSAGSLTIDASGLSSYELDPDLSERLRASVILAAPLLVRFGKAIVTPPGGDQIGERLLDTHFSMMKEFGVTVEAKDGKFHLDWEKKKAPRVFLEEASVTATEMGLILASSVSEEIVLEDAASEPHVQDLAKMLIKMGSKIDGAGTNRIAVSGKKKLLGVEHRVVPDHIDGGTFAIAAAITGGHVEIEDCPEEDYHLFLHYLKSMGVEAECEENNRLCVKPSNLRALKRKFQTRPWPGFPTDLMSPFIVLATQTEGTVLCHDWMYEWRVFFVDDLISMGANIFIADPHRVIVTGPTKLRGEKLFCKDIRAGISIILAALVARGTSVIDNVEMVERGYETIVER |
Sequence similarities
Belongs to the EPSP synthase family. MurA subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length981
- Mass (Da)106,537
- Last updated2015-07-22 v1
- Checksum239A2D6EF0D6D30C
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LCLV01000017 EMBL· GenBank· DDBJ | KKU23050.1 EMBL· GenBank· DDBJ | Genomic DNA |