HAMAP rule MF_01631
General rule information
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Accession | MF_01631 |
Dates | 4-APR-2006 (Created) 19-NOV-2022 (Last updated, Version 39) |
Name | GlmU |
Scope | Bacteria |
Templates | P0ACC7 (GLMU_ECOLI); Q97R46 (GLMU_STRPN); P9WMN3 (GLMU_MYCTU): [Recover all] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
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Protein name |
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Gene name |
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Comments
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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 | RHEA:13725: acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate
EC 2.3.1.157 |
RHEA:13509: H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
EC 2.7.7.23 |
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Cofactor | Mg(2+) Note: Binds 1 Mg(2+) 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. | |
Subunit | Homotrimer. |
Subcellular location | Cytoplasm. |
Similarity | 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
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Cytoplasm
Acyltransferase
Cell shape
Cell wall biogenesis/degradation
Magnesium
Metal-binding
Multifunctional enzyme
Nucleotidyltransferase
Peptidoglycan synthesis
Repeat
Transferase
Acyltransferase
Cell shape
Cell wall biogenesis/degradation
Magnesium
Metal-binding
Multifunctional enzyme
Nucleotidyltransferase
Peptidoglycan synthesis
Repeat
Transferase
Gene Ontology
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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.
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
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PROSITE | PS00101; HEXAPEP_TRANSFERASES; 1; |
Pfam | PF00132; Hexapep; 7; |
PF00483; NTP_transferase; 1; | |
PF01128; IspD; 1; | |
PF02348; CTP_transf_3; 1; | |
PRINTS | PR01590; HTHFIS; 1; |
PR01415; ANKYRIN; 1; | |
TIGRFAMs | TIGR01173; GlmU; 1; |
Features
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From: GLMU_ECOLI (P0ACC7) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
REGION | Nter | 229 | Pyrophosphorylase | |||||||||
BINDING (Optional) | 11 | 14 | /ligand="UDP-N-acetyl-alpha-D-glucosamine" /ligand_id="ChEBI:CHEBI:57705 | L-A-A-G | ||||||||
BINDING (Optional) | 81 | 82 | /ligand="UDP-N-acetyl-alpha-D-glucosamine" /ligand_id="ChEBI:CHEBI:57705 | G-T | ||||||||
BINDING (Optional) | 103 | 105 | /ligand="UDP-N-acetyl-alpha-D-glucosamine" /ligand_id="ChEBI:CHEBI:57705 | [SY]-G-D | ||||||||
REGION | 230 | 250 | Linker | |||||||||
REGION | 251 | Cter | N-acetyltransferase | |||||||||
BINDING (Optional) | 386 | 387 | /ligand="acetyl-CoA" /ligand_id="ChEBI:CHEBI:57288 | N-Y | ||||||||
ACT_SITE | 363 | 363 | 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 (Optional) | 25 | 25 | /ligand="UDP-N-acetyl-alpha-D-glucosamine" /ligand_id="ChEBI:CHEBI:57705 | K | ||||||||
BINDING (Optional) | 76 | 76 | /ligand="UDP-N-acetyl-alpha-D-glucosamine" /ligand_id="ChEBI:CHEBI:57705 | Q | ||||||||
BINDING (Optional) | 140 | 140 | /ligand="UDP-N-acetyl-alpha-D-glucosamine" /ligand_id="ChEBI:CHEBI:57705 | G | ||||||||
BINDING (Optional) | 154 | 154 | /ligand="UDP-N-acetyl-alpha-D-glucosamine" /ligand_id="ChEBI:CHEBI:57705 | E | ||||||||
BINDING (Optional) | 169 | 169 | /ligand="UDP-N-acetyl-alpha-D-glucosamine" /ligand_id="ChEBI:CHEBI:57705 | N | ||||||||
BINDING (Optional) | 227 | 227 | /ligand="UDP-N-acetyl-alpha-D-glucosamine" /ligand_id="ChEBI:CHEBI:57705 | N | ||||||||
BINDING (Optional) | 333 | 333 | /ligand="UDP-N-acetyl-alpha-D-glucosamine" /ligand_id="ChEBI:CHEBI:57705 | R | ||||||||
BINDING (Optional) | 351 | 351 | /ligand="UDP-N-acetyl-alpha-D-glucosamine" /ligand_id="ChEBI:CHEBI:57705 | K | ||||||||
BINDING (Optional) | 366 | 366 | /ligand="UDP-N-acetyl-alpha-D-glucosamine" /ligand_id="ChEBI:CHEBI:57705 | Y | ||||||||
BINDING (Optional) | 377 | 377 | /ligand="UDP-N-acetyl-alpha-D-glucosamine" /ligand_id="ChEBI:CHEBI:57705 | N | ||||||||
BINDING (Optional) | 380 | 380 | /ligand="acetyl-CoA" /ligand_id="ChEBI:CHEBI:57288 | A | ||||||||
BINDING (Optional) | 405 | 405 | /ligand="acetyl-CoA" /ligand_id="ChEBI:CHEBI:57288 | S | ||||||||
BINDING (Optional) | 423 | 423 | /ligand="acetyl-CoA" /ligand_id="ChEBI:CHEBI:57288 | [ACGST] | ||||||||
BINDING (Optional) | 440 | 440 | /ligand="acetyl-CoA" /ligand_id="ChEBI:CHEBI:57288 | R |
Additional information
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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. |