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HAMAP rule MF_01631

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General rule information [?]

Accession MF_01631
Dates 4-APR-2006 (Created)
1-JUN-2023 (Last updated, Version 40)
Name GlmU
Scope(s) Bacteria
Template(s) P0ACC7 (GLMU_ECOLI); Q97R46 (GLMU_STRPN); P9WMN3 (GLMU_MYCTU); [ Recover all ]
Triggered by HAMAP; MF_01631 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier GLMU
Protein name RecName: Full=Bifunctional protein GlmU;
                 Includes:
RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase;
                 EC=2.7.7.23;
AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase;
                 Includes:
RecName: Full=Glucosamine-1-phosphate N-acetyltransferase;
                 EC=2.3.1.157;
Gene name Name=glmU;

Comments [?]

FUNCTIONCatalyzes 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 Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N- acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157;
CATALYTIC ACTIVITY Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23;
COFACTOR Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.;
PATHWAYNucleotide-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.
PATHWAYNucleotide-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.
PATHWAYBacterial outer membrane biogenesis; LPS lipid A biosynthesis.
SUBUNITHomotrimer.
SUBCELLULAR LOCATIONCytoplasm.
SIMILARITYIn the N-terminal section; belongs to the N- acetylglucosamine-1-phosphate uridyltransferase family.
SIMILARITYIn the C-terminal section; belongs to the transferase hexapeptide repeat family.

Keywords [?]

Cytoplasm
Acyltransferase
Cell shape
Cell wall biogenesis/degradation
Magnesium
Metal-binding
Multifunctional enzyme
Nucleotidyltransferase
Peptidoglycan synthesis
Repeat
Transferase

Gene Ontology [?]

GO:0000287; Molecular function:magnesium ion binding
GO:0003977; Molecular function:UDP-N-acetylglucosamine diphosphorylase activity
GO:0019134; Molecular function:glucosamine-1-phosphate N-acetyltransferase activity
GO:0000902; Biological process:cell morphogenesis
GO:0009252; Biological process:peptidoglycan biosynthetic process
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

PROSITE PS00101; HEXAPEP_TRANSFERASES; 1;
Pfam PF00132; Hexapep; 7;
Pfam PF00483; NTP_transferase; 1;
Pfam PF01128; IspD; 1;
Pfam PF02348; CTP_transf_3; 1;
PRINTS PR01590; HTHFIS; 1;
PRINTS PR01415; ANKYRIN; 1;
NCBIfam TIGR01173; GlmU; 1;

Features [?]

From: GLMU_ECOLI (P0ACC7)
Key From To Description Tag Condition FTGroup
REGION Nter 229 /note="Pyrophosphorylase"
BINDING 11 14 /ligand="UDP-N-acetyl-alpha-D-glucosamine"
/ligand_id="ChEBI:CHEBI:57705"		 L-A-A-G
BINDING 81 82 /ligand="UDP-N-acetyl-alpha-D-glucosamine"
/ligand_id="ChEBI:CHEBI:57705"		 G-T
BINDING 103 105 /ligand="UDP-N-acetyl-alpha-D-glucosamine"
/ligand_id="ChEBI:CHEBI:57705"		 [SY]-G-D
REGION 230 250 /note="Linker"
REGION 251 Cter /note="N-acetyltransferase"
BINDING 386 387 /ligand="acetyl-CoA"
/ligand_id="ChEBI:CHEBI:57288"		 N-Y
ACT_SITE 363 363 /note="Proton acceptor" H
BINDING 105 105 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"		 D
BINDING 227 227 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"		 N
BINDING 25 25 /ligand="UDP-N-acetyl-alpha-D-glucosamine"
/ligand_id="ChEBI:CHEBI:57705"		 K
BINDING 76 76 /ligand="UDP-N-acetyl-alpha-D-glucosamine"
/ligand_id="ChEBI:CHEBI:57705"		 Q
BINDING 140 140 /ligand="UDP-N-acetyl-alpha-D-glucosamine"
/ligand_id="ChEBI:CHEBI:57705"		 G
BINDING 154 154 /ligand="UDP-N-acetyl-alpha-D-glucosamine"
/ligand_id="ChEBI:CHEBI:57705"		 E
BINDING 169 169 /ligand="UDP-N-acetyl-alpha-D-glucosamine"
/ligand_id="ChEBI:CHEBI:57705"		 N
BINDING 227 227 /ligand="UDP-N-acetyl-alpha-D-glucosamine"
/ligand_id="ChEBI:CHEBI:57705"		 N
BINDING 333 333 /ligand="UDP-N-acetyl-alpha-D-glucosamine"
/ligand_id="ChEBI:CHEBI:57705"		 R
BINDING 351 351 /ligand="UDP-N-acetyl-alpha-D-glucosamine"
/ligand_id="ChEBI:CHEBI:57705"		 K
BINDING 366 366 /ligand="UDP-N-acetyl-alpha-D-glucosamine"
/ligand_id="ChEBI:CHEBI:57705"		 Y
BINDING 377 377 /ligand="UDP-N-acetyl-alpha-D-glucosamine"
/ligand_id="ChEBI:CHEBI:57705"		 N
BINDING 380 380 /ligand="acetyl-CoA"
/ligand_id="ChEBI:CHEBI:57288"		 A
BINDING 405 405 /ligand="acetyl-CoA"
/ligand_id="ChEBI:CHEBI:57288"		 S
BINDING 423 423 /ligand="acetyl-CoA"
/ligand_id="ChEBI:CHEBI:57288"		 [ACGST]
BINDING 440 440 /ligand="acetyl-CoA"
/ligand_id="ChEBI:CHEBI:57288"		 R

Additional information [?]

Size range 339-500 amino acids
Related rules None
Fusion Nter: None Cter: <PPC domain>
Comments SYNJA and SYNJB are fusioned in their C-terminal parts to a PPC domain.



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