A6VKY9 · MURQ_ACTSZ
- ProteinN-acetylmuramic acid 6-phosphate etherase
- GenemurQ
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids304 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate. Together with AnmK, is also required for the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
Miscellaneous
A lyase-type mechanism (elimination/hydration) is suggested for the cleavage of the lactyl ether bond of MurNAc 6-phosphate, with the formation of an alpha,beta-unsaturated aldehyde intermediate with (E)-stereochemistry, followed by the syn addition of water to give product.
Catalytic activity
- H2O + N-acetyl-D-muramate 6-phosphate = (R)-lactate + N-acetyl-D-glucosamine 6-phosphate
Pathway
Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
Amino-sugar metabolism; N-acetylmuramate degradation.
Cell wall biogenesis; peptidoglycan recycling.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 90 | Proton donor | ||||
Sequence: E | ||||||
Active site | 121 | |||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | carbohydrate binding | |
Molecular Function | carbon-oxygen lyase activity | |
Molecular Function | enzyme binding | |
Molecular Function | enzyme inhibitor activity | |
Molecular Function | fructose-6-phosphate binding | |
Biological Process | 1,6-anhydro-N-acetyl-beta-muramic acid catabolic process | |
Biological Process | amino sugar catabolic process | |
Biological Process | glucose homeostasis | |
Biological Process | N-acetylmuramic acid catabolic process | |
Biological Process | peptidoglycan turnover | |
Biological Process | response to fructose |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameN-acetylmuramic acid 6-phosphate etherase
- EC number
- Short namesMurNAc-6-P etherase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pasteurellales > Pasteurellaceae > Actinobacillus
Accessions
- Primary accessionA6VKY9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000071171 | 1-304 | N-acetylmuramic acid 6-phosphate etherase | |||
Sequence: MTEQNLLQSLAQMVTEQRNANSIDIDRLNAAEIVKIINQEDKSVPFAVEQCLPQIALAVEKIVTAFRQGGRLVYIGAGTSGRLGVLDASECPPTYGVPSDMVVGIIAGGERALRHPIEGAEDNPQQGQADLENIHFTAKDVLVGIAASGRTPYVIGALNYAKSLDAVTVAITGNPGSAMTQIADIAIEAVVGQEVLTGSSRMKSGTAQKLVLNMLTTASMILMGKCYQNLMVDVQASNEKLRARAVRIVMQATECSKDVAQETLQRADNNAKLAIMMVLSGLEKTDAAQVLDRHQGKLRQALAQ |
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 62-225 | SIS | ||||
Sequence: IVTAFRQGGRLVYIGAGTSGRLGVLDASECPPTYGVPSDMVVGIIAGGERALRHPIEGAEDNPQQGQADLENIHFTAKDVLVGIAASGRTPYVIGALNYAKSLDAVTVAITGNPGSAMTQIADIAIEAVVGQEVLTGSSRMKSGTAQKLVLNMLTTASMILMGK |
Sequence similarities
Belongs to the GCKR-like family. MurNAc-6-P etherase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length304
- Mass (Da)32,440
- Last updated2007-08-21 v1
- ChecksumDA7FC464E997DCD4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000746 EMBL· GenBank· DDBJ | ABR73636.1 EMBL· GenBank· DDBJ | Genomic DNA |