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HAMAP annotation rule: MF_01631

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General rule information

Accession MF_01631
Dates 4-APR-2006 (Created)
7-JUN-2008 (Last updated, Version 23)
Data class Protein
Predictors HAMAP; MF_01631; [distribution of match scores in UniProtKB];[seed alignment for MF_01631]


Propagated annotation

Identifier, protein and gene names
Identifier GLMU
Protein name
RecName: Full=Bifunctional protein glmU;
RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase;
EC=2.7.7.23;
AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase;
RecName: Full=Glucosamine-1-phosphate N-acetyltransferase;
EC=2.3.1.157;
Gene name glmU
Comments
FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-GlcNAc. Responsible for the acetylation of Glc-N-1-P to give GlcNAc-1-P and for the uridyl transfer from UTP to GlcNAc-1-P which produces UDP-GlcNAc (By similarity).
CATALYTIC ACTIVITY: Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate.
CATALYTIC ACTIVITY: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-D-glucosamine.
COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from D-glucosamine 6-phosphate (route II): step 2/2.
PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-D-glucosamine biosynthesis; UDP-N-acetyl-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
PATHWAY: Context: Lipopolysaccharide (LPS) biosynthesis; lipid A biosynthesis.
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.
SIMILARITY: In the C-terminal section; belongs to the transferase hexapeptide repeat family.
Cross-references
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;
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.
Features
From: GLMU_ECOLI (P0ACC7)
Key     From     To       Description   Condition   FTGroup
REGION     Nter     229       Pyrophosphorylase (By similarity)      
REGION (Optional)     11     14       Substrate binding (By similarity)   L-A-A-G  
REGION (Optional)     81     82       Substrate binding (By similarity)   G-T  
REGION     230     250       Linker (By similarity)      
REGION     251     Cter       N-acetyltransferase (By similarity)      
METAL     105     105       Magnesium (By similarity)   D  
METAL     227     227       Magnesium (By similarity)   N  
ACT_SITE     363     363       Proton acceptor (By similarity)   H  
BINDING (Optional)     76     76       Substrate (By similarity)   Q  
BINDING (Optional)     140     140       Substrate; via amide nitrogen (By similarity)   G  
BINDING (Optional)     154     154       Substrate (By similarity)   E  
BINDING (Optional)     169     169       Substrate (By similarity)   N  
BINDING (Optional)     387     387       Acetyl-CoA (By similarity)   Y  
BINDING (Optional)     405     405       Acetyl-CoA (By similarity)   S  
BINDING (Optional)     423     423       Acetyl-CoA; via amide nitrogen (By similarity)   [ACGST]  
BINDING (Optional)     440     440       Acetyl-CoA (By similarity)   R  


Additional information

Size range: 339-500 amino acids
Related UniRules: None
Template: P0ACC7 (GLMU_ECOLI); Q97R46 (GLMU_STRPN): [Recover all]
Scope: Bacteria
Fusion: Nter: None; Cter: <Unknown>
Duplicate: None
Plasmid encoded: None
Comments: SYNJA and SYNJB are fusioned in their C-terminal parts to an unknown domain.

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UniProtKB rule member sequences



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