A0A3T3GDL1 · A0A3T3GDL1_SALET

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

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.

TypeIDPosition(s)Description
Binding site11-14UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site25UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site76UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site81-82UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site103-105UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site105Mg2+ (UniProtKB | ChEBI)
Binding site140UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site154UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site169UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site227Mg2+ (UniProtKB | ChEBI)
Binding site227UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site333UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site351UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Active site363Proton acceptor
Binding site366UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site377UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site380acetyl-CoA (UniProtKB | ChEBI)
Binding site386-387acetyl-CoA (UniProtKB | ChEBI)
Binding site405acetyl-CoA (UniProtKB | ChEBI)
Binding site423acetyl-CoA (UniProtKB | ChEBI)
Binding site440acetyl-CoA (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionglucosamine-1-phosphate N-acetyltransferase activity
Molecular Functionmagnesium ion binding
Molecular FunctionUDP-N-acetylglucosamine diphosphorylase activity
Biological Processcell morphogenesis
Biological Processcell wall organization
Biological Processlipid A biosynthetic process
Biological Processpeptidoglycan biosynthetic process
Biological Processregulation of cell shape
Biological ProcessUDP-N-acetylglucosamine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Bifunctional protein GlmU

Including 2 domains:

  • Recommended name
    UDP-N-acetylglucosamine pyrophosphorylase
  • EC number
  • Alternative names
    • N-acetylglucosamine-1-phosphate uridyltransferase
  • Recommended name
    Glucosamine-1-phosphate N-acetyltransferase
  • EC number

Gene names

    • Name
      glmU
    • ORF names
      A4W49_20395
      , A4W57_19710
      , AIK92_20675
      , ASH82_08770
      , CB395_18645
      , CIL65_14575
      , D6J51_20430
      , D6K67_21445
      , DKU10_20005
      , DOJ23_10320
      , DP829_21460
      , DPJ44_21300
      , DPS10_20050
      , DQQ63_18370
      , DY868_22055
      , EUX26_21000
      , F9G64_15100
      , G0D76_10285
      , G3408_004314
      , G4B28_002950
      , G4B35_003416
      , G4I58_004135
      , G4I61_001368
      , G4L02_004297
      , G4Y23_004220
      , G9C15_002346
      , GCZ77_21610

Organism names

Accessions

  • Primary accession
    A0A3T3GDL1
  • Secondary accessions
    • A0A6C8XQ24

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotrimer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-229Pyrophosphorylase
Domain8-120MobA-like NTP transferase
Region230-250Linker
Region251-456N-acetyltransferase

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    456
  • Mass (Da)
    49,180
  • Last updated
    2019-05-08 v1
  • Checksum
    D0C8057D43A3826B
MLNSAMSVVILAAGKGTRMYSDIPKVLHTLAGKPMVQHVIDAATKLGAAQVHLVYGHGGELLKQTLKDDKLNWVLQAEQLGTGHAMQQAAPFFSDDEDILMLYGDVPLISVETLQRLRDAKPQGGIGLLTVKLDDPSGYGRITRENGKVTGIVEHKDATDEQRQIQEINTGILIANGADLKRWLSKLTNNNAQGEYYITDIIALAYQEGREIAAVHPARISETDGVNNRLQLSRLERIYQAEQAEKLLLSGVMLRDPARFDLRGTLHCGMDVEIDANVIIEGYVTLGHRVKIGAGCIIKNSVIGDDCEISPYSVVEDAHLEAACTIGPFARLRPGAELLAGAHVGNFVEMKKARLGKGSKAGHLTYLGDAEIGDNVNIGAGTITCNYDGANKFKTVIGDDVFVGSDTQLVAPVTVGKGATIAAGTTVTRNVADNELVLSRVPQVHKQGWQRPVKKK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Similar Proteins

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