Q9ZLF6 · GLMU_HELPJ

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

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Pathway

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.
Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site7-10UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site21UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site80-81UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site106Mg2+ (UniProtKB | ChEBI)
Binding site138UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site152UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site167UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site224Mg2+ (UniProtKB | ChEBI)
Binding site224UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site311UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site328UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Active site339Proton acceptor
Binding site342UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site353UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site356acetyl-CoA (UniProtKB | ChEBI)
Binding site362-363acetyl-CoA (UniProtKB | ChEBI)
Binding site381acetyl-CoA (UniProtKB | ChEBI)
Binding site399acetyl-CoA (UniProtKB | ChEBI)
Binding site416acetyl-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

    • UPA00113UER00532
    • UPA00113UER00533
    • UPA00973

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
    • Ordered locus names
      jhp_0624

Organism names

Accessions

  • Primary accession
    Q9ZLF6

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002337831-433Bifunctional protein GlmU

Interaction

Subunit

Homotrimer.

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-226Pyrophosphorylase
Region227-247Linker
Region248-433N-acetyltransferase

Sequence similarities

In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.
In the C-terminal section; belongs to the transferase hexapeptide repeat family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    433
  • Mass (Da)
    47,883
  • Last updated
    1999-05-01 v1
  • Checksum
    D2EFE3DFC0485BDE
MLSVIILAAGKGTRMHSSLPKTLHTICGEPMLFYILEVAFSISNDVHLVLHHQQERIKEAVSKRFKGVIFHAQIVEKYSGTGGAIMQENKTPIPTQHERVLILNADMPLITKDALTPLLESHNNAIGLLHLADPKGYGRVILENHQVKKIVEEKDANDEEKTIKSVNAGVYFFERKFLERYLPKLHDQNAQKEYYLTDLIALGIKGNEKIDAIFLEEECFLGVNSQTERAKAEEIMLERLRKNAMDLGVVMQLPSSIYLEKGVSFKGECVLEQGVRLIGNCLIENARIKAYSVIEESQIINSSVGPFAHARPKSVICDSHVGNFVETKNAKLQGTKAGHLSYLGDCEIGKNTNVGAGVITCNYDGKKKHQTIIGENVFIGSDSQLVAPINIGSNVLIGSGTTITKDIPSGSLSLSRTPQTNIENGYFKFFKKP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE001439
EMBL· GenBank· DDBJ
AAD06204.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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