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Enzyme Nomenclature
Information on EC 2.7.7.99 - N-acetyl-alpha-D-muramate 1-phosphate uridylyltransferase
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The expected taxonomic range for this enzyme is: Pseudomonas putida
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EC NUMBER 
COMMENTARY 
2.7.7.99
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RECOMMENDED NAME
GeneOntology No.
N-acetyl-alpha-D-muramate 1-phosphate uridylyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP + N-acetyl-alpha-D-muramate 1-phosphate = UDP-N-acetyl-alpha-D-muramate + phosphate
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
UDP:N-acetyl-alpha-D-muramate 1-phosphate uridylyltransferase
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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the metabolic pathway of anomeric cell wall amino sugar kinase AmgK and uridylyl transferase MurU converts N-acetylmuramic acid to uridine diphosphate-N-acetylmuramic acid. It is responsible for the high intrinsic resistance of Pseudomonas aeruginosa to fosfomycin due to bypassing the fosfomycin-sensitive de novo synthesis of UDP-N-acetylmuramic acid
physiological function
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enzyme is involved in a salvage pathway in Gram-negative bacteria that bypasses de novo biosynthesis of UDP N-acetylmuramic acid. The pathway consisits of anomeric sugar kinase AmgK and the MurNAc alpha-1-phosphate uridylyl transferase MurU. Deletion of the encoding gene increases fosfomycin sensitivity
physiological function
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enzyme is involved in a salvage pathway in Gram-negative bacteria that bypasses de novo biosynthesis of UDP N-acetylmuramic acid. The pathway consisits of anomeric sugar kinase AmgK and the MurNAc alpha-1-phosphate uridylyl transferase MurU. Deletion of the encoding gene increases fosfomycin sensitivity; the metabolic pathway of anomeric cell wall amino sugar kinase AmgK and uridylyl transferase MurU converts N-acetylmuramic acid to uridine diphosphate-N-acetylmuramic acid. It is responsible for the high intrinsic resistance of Pseudomonas aeruginosa to fosfomycin due to bypassing the fosfomycin-sensitive de novo synthesis of UDP-N-acetylmuramic acid
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UTP + N-acetyl-alpha-D-muramate 1-phosphate
UDP-N-acetyl-alpha-D-muramate + diphosphate
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?
UTP + N-acetyl-alpha-D-muramate 1-phosphate
UDP-N-acetyl-alpha-D-muramate + diphosphate
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?
UTP + N-acetyl-alpha-D-muramate 1-phosphate
UDP-N-acetyl-alpha-D-muramate + diphosphate
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-
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?
UTP + N-acetyl-alpha-D-muramate 1-phosphate
UDP-N-acetyl-alpha-D-muramate + diphosphate
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?
additional information
?
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no substrates: ATP, CTP, TTP, or GTP
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additional information
?
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no substrates: N-acetyl-D-glucosamine 1-phosphate, N-acetyl-D-galactosamine 1-phosphate
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additional information
?
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no substrates: ATP, CTP, TTP, or GTP
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additional information
?
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no substrates: N-acetyl-D-glucosamine 1-phosphate, N-acetyl-D-galactosamine 1-phosphate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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two Mg2+ ions are likely part of the active site. Mg2+ is not required for substrate binding per se
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440);
Q88QT2
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440);
Q88QT2
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440);
Q88QT2
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures of MurU in native and ligand-bound states at 1.8 A resolution
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LINKS TO OTHER DATABASES (specific for EC-Number 2.7.7.99)
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