AC MF_01631; DC Protein; auto TR HAMAP; MF_01631; -; 1; level=0 XX Names: GlmU XX ID GLMU DE RecName: Full=Bifunctional protein GlmU; DE Includes: DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase; DE EC=2.7.7.23; DE AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase; DE Includes: DE RecName: Full=Glucosamine-1-phosphate N-acetyltransferase; DE EC=2.3.1.157; GN Name=glmU; XX CC -!- FUNCTION: Catalyzes the last two sequential reactions in the de novo CC biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- CC terminal domain catalyzes the transfer of acetyl group from acetyl CC coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- CC acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into CC UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- CC triphosphate), a reaction catalyzed by the N-terminal domain. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N- CC acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = CC diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, CC ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 Mg(2+) ion per subunit.; CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D- CC glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from CC alpha-D-glucosamine 6-phosphate (route II): step 2/2. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D- CC glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N- CC acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. CC -!- SUBUNIT: Homotrimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: In the N-terminal section; belongs to the N- CC acetylglucosamine-1-phosphate uridyltransferase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase CC hexapeptide repeat family. XX DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1; trigger=no DR Pfam; PF00132; Hexapep; 7; trigger=no DR Pfam; PF00483; NTP_transferase; 1; trigger=no DR Pfam; PF01128; IspD; 1; trigger=no DR Pfam; PF02348; CTP_transf_3; 1; trigger=no DR PRINTS; PR01590; HTHFIS; 1; trigger=no DR PRINTS; PR01415; ANKYRIN; 1; trigger=no DR NCBIfam; TIGR01173; GlmU; 1; trigger=no XX KW Cytoplasm KW Acyltransferase KW Cell shape KW Cell wall biogenesis/degradation KW Magnesium KW Metal-binding KW Multifunctional enzyme KW Nucleotidyltransferase KW Peptidoglycan synthesis KW Repeat KW Transferase XX GO GO:0000287; F:magnesium ion binding GO GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity GO GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity GO GO:0000902; P:cell morphogenesis GO GO:0009252; P:peptidoglycan biosynthetic process GO GO:0005737; C:cytoplasm XX FT From: GLMU_ECOLI (P0ACC7) FT REGION Nter..229 FT /note="Pyrophosphorylase" FT BINDING 11..14 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT Optional; Condition: L-A-A-G FT BINDING 81..82 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT Optional; Condition: G-T FT BINDING 103..105 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT Optional; Condition: [SY]-G-D FT REGION 230..250 FT /note="Linker" FT REGION 251..Cter FT /note="N-acetyltransferase" FT BINDING 386..387 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT Optional; Condition: N-Y FT ACT_SITE 363 FT /note="Proton acceptor" FT Condition: H FT BINDING 105 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: D FT BINDING 227 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: N FT BINDING 25 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT Optional; Condition: K FT BINDING 76 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT Optional; Condition: Q FT BINDING 140 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT Optional; Condition: G FT BINDING 154 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT Optional; Condition: E FT BINDING 169 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT Optional; Condition: N FT BINDING 227 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT Optional; Condition: N FT BINDING 333 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT Optional; Condition: R FT BINDING 351 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT Optional; Condition: K FT BINDING 366 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT Optional; Condition: Y FT BINDING 377 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT Optional; Condition: N FT BINDING 380 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT Optional; Condition: A FT BINDING 405 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT Optional; Condition: S FT BINDING 423 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT Optional; Condition: [ACGST] FT BINDING 440 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT Optional; Condition: R XX Size: 339-500; Related: None; Template: P0ACC7; Q97R46; P9WMN3; Scope: Bacteria Fusion: Nter: None Cter: Duplicate: None Plasmid: None Comments: SYNJA and SYNJB are fusioned in their C-terminal parts to a PPC domain. XX # Revision 1.40 2023/06/01 //