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Information on EC 2.7.8.35 - UDP-N-acetylglucosamine-decaprenyl-phosphate N-acetylglucosaminephosphotransferase and Organism(s) Mycolicibacterium smegmatis and UniProt Accession A0R211

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IUBMB Comments
Isolated from Mycobacterium tuberculosis and Mycobacterium smegmatis. This enzyme catalyses the synthesis of monotrans,octacis-decaprenyl-N-acetyl-alpha-D-glucosaminyl diphosphate (mycobacterial lipid I), an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components. cf. EC 2.7.8.33, UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase.
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Mycolicibacterium smegmatis
UNIPROT: A0R211
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The taxonomic range for the selected organisms is: Mycolicibacterium smegmatis
The enzyme appears in selected viruses and cellular organisms
Synonyms
glcnac-1-phosphate transferase, msmeg_4947, rv1302, polyprenyl phosphate-glcnac-1-phosphate transferase, udp-glcnac undecaprenyl phosphate glcnac-1-phosphate transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MSMEG_4947
locus name
N-acetylglucosamine-1-phosphate transferase
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polyprenyl phosphate-GlcNAc-1-phosphate transferase
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GlcNAc-1-phosphate transferase
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-
-
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UDP-GlcNAc: undecaprenyl phosphate GlcNAc-1-phosphate transferase
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UDP-GlcNAc:undecaprenyl phosphate GlcNAc-1-phosphate transferase
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-
-
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WecA transferase
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-
-
-
PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine:trans,octacis-decaprenyl-phosphate N-acetylglucosaminephosphotransferase
Isolated from Mycobacterium tuberculosis and Mycobacterium smegmatis. This enzyme catalyses the synthesis of monotrans,octacis-decaprenyl-N-acetyl-alpha-D-glucosaminyl diphosphate (mycobacterial lipid I), an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components. cf. EC 2.7.8.33, UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase.
CAS REGISTRY NUMBER
COMMENTARY hide
313355-28-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine + trans,octacis-decaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol
show the reaction diagram
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + trans,octacis-decaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol
show the reaction diagram
-
-
-
-
r
additional information
?
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specificity of WecA against truncated prenyl phosphates, overview. Decaprenyl phosphate and undecaprenyl phosphate are equally effective, no activity with substrates that have shorter prenyl chains
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine + trans,octacis-decaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DMSO
50% inhibition at 10% v/v, no inhibition at 2.86% v/v
Rifampin
the sensitivity of wild-type mc2155 strain against rifampin is enhanced in the presence of low concentrations of tunicamycin, a natural WecA inhibitor. An enzyme knockdown mutant strain also shows increased sensitivity to rifampin
additional information
synthesis and evaluation of a series of capuramycin analogues as WecA enzyme inhibitors. No inhibition by capuramycin, UT-01309, and SQ641
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten enzyme kinetics
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Mycolicibacterium smegmatis
IC50 for tunicamycin is 590 ng/ml at pH 8.0 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene wecA
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
a Mycobacterium smegmatis wecA knockdown strain regulated by antisense RNA has a decreased growth rate and the amount of live bacterial cells drops. In addition, the wecA knockdown strain exhibits dramatically morphological alterations. The wecA knockdown strain is more sensitive to rifampin, compared with the wecA normal-expression strain
physiological function
wecA is an essential gene for mycobacterial growth
malfunction
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the disruption of MSMEG 4947 in the Mycobaterium smegmatis genome results in the loss of viability at 42°C and causes drastic morphological changes like pear shape and larger diameter
metabolism
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the enzyme catalyzes the first step in the biosynthesis of lipopolysaccharide O-antigen
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
construction of a Mycobacterium smegmatis wecA knockdown strain by using a tetracycline-inducible expression vector pMind, the expression of WecA is regulated by antisense RNA
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
preparation of membrane fraction
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in wecA-defective Escherichia coli MV501 cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jin, Y.; Xin, Y.; Zhang, W.; Ma, Y.
Mycobacterium tuberculosis Rv1302 and Mycobacterium smegmatis MSMEG 4947 have WecA function and MSMEG 4947 is required for the growth of M. smegmatis
FEMS Microbiol. Lett.
310
54-61
2010
Mycobacterium tuberculosis, Mycolicibacterium smegmatis, Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
Manually annotated by BRENDA team
Mitachi, K.; Siricilla, S.; Yang, D.; Kong, Y.; Skorupinska-Tudek, K.; Swiezewska, E.; Franzblau, S.G.; Kurosu, M.
Fluorescence-based assay for polyprenyl phosphate-GlcNAc-1-phosphate transferase (WecA) and identification of novel antimycobacterial WecA inhibitors
Anal. Biochem.
512
78-90
2016
Escherichia coli (P0AC78), Mycobacterium tuberculosis (P9WMW5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WMW5), Mycolicibacterium smegmatis (A0R211), Mycolicibacterium smegmatis mc(2)155 / ATCC 700084 (A0R211)
Manually annotated by BRENDA team
Xu, L.; Qian, L.; Kang, J.; Sha, S.; Xin, Y.; Lu, S.; Ma, Y.
Down-regulation of N-acetylglucosamine-1-phosphate transferase (WecA) enhanced the sensitivity of Mycobacterium smegmatis against rifampin
J. Appl. Microbiol.
121
966-972
2016
Mycolicibacterium smegmatis (A0R211), Mycolicibacterium smegmatis mc(2)155 / ATCC 700084 (A0R211)
Manually annotated by BRENDA team