F0GZJ6 · F0GZJ6_9FIRM
- ProteinBifunctional protein GlmU
- GeneglmU
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids791 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
Catalytic activity
- D-ribose 5-phosphate + ATP = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H+
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Mg2+ ion per subunit.
Note: Binds 2 Mg2+ ions per subunit.
Pathway
Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1.
Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 7-10 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 21 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 78-79 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 102 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 139 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 153 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 168 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 226 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 226 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 331 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 349 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Active site | 361 | Proton acceptor | |||
Binding site | 364 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 375 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 384-385 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 403 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 421 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 438 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 512-514 | ATP (UniProtKB | ChEBI) | |||
Binding site | 571-572 | ATP (UniProtKB | ChEBI) | |||
Binding site | 605 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 646 | Mg2+ (UniProtKB | ChEBI) | |||
Active site | 669 | ||||
Binding site | 671 | D-ribose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 695 | D-ribose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 699-703 | D-ribose 5-phosphate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | ribose phosphate diphosphokinase complex | |
Molecular Function | ATP binding | |
Molecular Function | glucosamine-1-phosphate N-acetyltransferase activity | |
Molecular Function | kinase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | ribose phosphate diphosphokinase activity | |
Molecular Function | UDP-N-acetylglucosamine diphosphorylase activity | |
Biological Process | 5-phosphoribose 1-diphosphate biosynthetic process | |
Biological Process | cell morphogenesis | |
Biological Process | cell wall organization | |
Biological Process | lipid A biosynthetic process | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | phosphorylation | |
Biological Process | purine nucleotide biosynthetic process | |
Biological Process | regulation of cell shape | |
Biological Process | ribonucleoside monophosphate biosynthetic process | |
Biological Process | UDP-N-acetylglucosamine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBifunctional protein GlmU
Including 2 domains:
- Recommended nameUDP-N-acetylglucosamine pyrophosphorylase
- EC number
- Alternative names
- Recommended nameGlucosamine-1-phosphate N-acetyltransferase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Tissierellia > Tissierellales > Peptoniphilaceae > Anaerococcus
Accessions
- Primary accessionF0GZJ6
Proteomes
Subcellular Location
Interaction
Subunit
Homohexamer.
Homotrimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-228 | Pyrophosphorylase | |||
Domain | 3-216 | Nucleotidyl transferase | |||
Region | 229-249 | Linker | |||
Region | 250-791 | N-acetyltransferase | |||
Domain | 479-595 | Ribose-phosphate pyrophosphokinase N-terminal | |||
Sequence similarities
Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.
In the C-terminal section; belongs to the transferase hexapeptide repeat family.
In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length791
- Mass (Da)87,390
- Last updated2011-05-03 v1
- MD5 ChecksumFBE304E553CF217B210E492128FFFE04
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AEXN01000011 EMBL· GenBank· DDBJ | EGC84507.1 EMBL· GenBank· DDBJ | Genomic DNA |