A0A3T3GDL1 · A0A3T3GDL1_SALET
- ProteinBifunctional protein GlmU
- GeneglmU
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids456 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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.
Catalytic activity
- H+ + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Pathway
Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
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 | 11-14 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: LAAG | ||||||
Binding site | 25 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 76 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 81-82 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: GT | ||||||
Binding site | 103-105 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: YGD | ||||||
Binding site | 105 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 140 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 154 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 169 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 227 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 227 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 333 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 351 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 363 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 366 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 377 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 380 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 386-387 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: NY | ||||||
Binding site | 405 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 423 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 440 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | glucosamine-1-phosphate N-acetyltransferase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | UDP-N-acetylglucosamine diphosphorylase activity | |
Biological Process | cell morphogenesis | |
Biological Process | cell wall organization | |
Biological Process | lipid A biosynthetic process | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | regulation of cell shape | |
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
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionA0A3T3GDL1
- Secondary accessions
Proteomes
Subcellular Location
Interaction
Subunit
Homotrimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-229 | Pyrophosphorylase | ||||
Sequence: MLNSAMSVVILAAGKGTRMYSDIPKVLHTLAGKPMVQHVIDAATKLGAAQVHLVYGHGGELLKQTLKDDKLNWVLQAEQLGTGHAMQQAAPFFSDDEDILMLYGDVPLISVETLQRLRDAKPQGGIGLLTVKLDDPSGYGRITRENGKVTGIVEHKDATDEQRQIQEINTGILIANGADLKRWLSKLTNNNAQGEYYITDIIALAYQEGREIAAVHPARISETDGVNNR | ||||||
Domain | 8-120 | MobA-like NTP transferase | ||||
Sequence: VVILAAGKGTRMYSDIPKVLHTLAGKPMVQHVIDAATKLGAAQVHLVYGHGGELLKQTLKDDKLNWVLQAEQLGTGHAMQQAAPFFSDDEDILMLYGDVPLISVETLQRLRDA | ||||||
Region | 230-250 | Linker | ||||
Sequence: LQLSRLERIYQAEQAEKLLLS | ||||||
Region | 251-456 | N-acetyltransferase | ||||
Sequence: GVMLRDPARFDLRGTLHCGMDVEIDANVIIEGYVTLGHRVKIGAGCIIKNSVIGDDCEISPYSVVEDAHLEAACTIGPFARLRPGAELLAGAHVGNFVEMKKARLGKGSKAGHLTYLGDAEIGDNVNIGAGTITCNYDGANKFKTVIGDDVFVGSDTQLVAPVTVGKGATIAAGTTVTRNVADNELVLSRVPQVHKQGWQRPVKKK |
Sequence similarities
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
Family and domain databases
Sequence
- Sequence statusComplete
- Length456
- Mass (Da)49,180
- Last updated2019-05-08 v1
- ChecksumD0C8057D43A3826B
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAHCWL010000023 EMBL· GenBank· DDBJ | EBU6916958.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHFAS010000018 EMBL· GenBank· DDBJ | EBV3761939.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHGTQ010000007 EMBL· GenBank· DDBJ | EBV9200709.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHIGD010000020 EMBL· GenBank· DDBJ | EBW4106618.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHIXO010000019 EMBL· GenBank· DDBJ | EBW6734355.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHKXZ010000021 EMBL· GenBank· DDBJ | EBX3357117.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHOXC010000020 EMBL· GenBank· DDBJ | EBY7386864.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHPAD010000020 EMBL· GenBank· DDBJ | EBY7628958.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHWIJ010000019 EMBL· GenBank· DDBJ | ECB0525620.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAKLND010000026 EMBL· GenBank· DDBJ | ECT0411972.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAKPQX010000018 EMBL· GenBank· DDBJ | ECU3485328.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAKTKA010000024 EMBL· GenBank· DDBJ | ECV4807077.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AALIQJ010000024 EMBL· GenBank· DDBJ | EDA0176166.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AALLSV010000021 EMBL· GenBank· DDBJ | EDA9403869.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AALLTD010000021 EMBL· GenBank· DDBJ | EDA9439012.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAMGJL010000013 EMBL· GenBank· DDBJ | EDH0980748.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAMIHV010000024 EMBL· GenBank· DDBJ | EDH6430827.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAAMJL010000003 EMBL· GenBank· DDBJ | HAC6915578.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAARLP010000012 EMBL· GenBank· DDBJ | HAE2915119.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAARUC010000020 EMBL· GenBank· DDBJ | HAE3940948.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAARUZ010000025 EMBL· GenBank· DDBJ | HAE4050253.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAASLG010000014 EMBL· GenBank· DDBJ | HAE6002467.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAASLQ010000015 EMBL· GenBank· DDBJ | HAE6031251.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAASRW010000013 EMBL· GenBank· DDBJ | HAE6748502.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAATPN010000014 EMBL· GenBank· DDBJ | HAE9563412.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAAUAM010000022 EMBL· GenBank· DDBJ | HAF0863154.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
RSGD01000020 EMBL· GenBank· DDBJ | MID47321.1 EMBL· GenBank· DDBJ | Genomic DNA |