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Information on EC 2.4.2.43 - lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase and Organism(s) Escherichia coli and UniProt Accession P76473

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.43 lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase
IUBMB Comments
Integral membrane protein present in the inner membrane of certain Gram negative endobacteria. In strains that do not produce 3-deoxy-D-manno-octulosonic acid (Kdo), the enzyme adds a single arabinose unit to the 1-phosphate moiety of the tetra-acylated lipid A precursor, lipid IVA. In the presence of a Kdo disaccharide, the enzyme primarily adds an arabinose unit to the 4-phosphate of lipid A molecules. The Salmonella typhimurium enzyme can add arabinose units to both positions.
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This record set is specific for:
Escherichia coli
UNIPROT: P76473
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Word Map
  • 2.4.2.43
  • photosystem
  • synechocystis
  • cyanobacterium
  • polymyxin
  • time-resolved
  • photoautotrophically
  • elongatus
  • epr
  • aeruginosa
  • thermosynechococcus
  • typhimurium
  • polymyxin-resistance
  • light-regulated
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
4-amino-4-deoxy-l-arabinose transferase, l-ara4n transferase, aminoarabinose transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
4-amino-4-deoxy-alpha-L-2-aminoarabinopyranosyl ditrans,octacis-undecaprenyl phosphate:lipid IVA L-2-aminoarabinopyranosyltransferase
Integral membrane protein present in the inner membrane of certain Gram negative endobacteria. In strains that do not produce 3-deoxy-D-manno-octulosonic acid (Kdo), the enzyme adds a single arabinose unit to the 1-phosphate moiety of the tetra-acylated lipid A precursor, lipid IVA. In the presence of a Kdo disaccharide, the enzyme primarily adds an arabinose unit to the 4-phosphate of lipid A molecules. The Salmonella typhimurium enzyme can add arabinose units to both positions.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,poly-cis-undecaprenyl phosphate + lipid IVA
lipid IIA + di-trans,poly-cis-undecaprenyl phosphate
show the reaction diagram
4-amino-4-deoxy-alpha-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[4-P-L-Ara4N]-lipid A + ditrans,octacis-undecaprenyl phosphate
show the reaction diagram
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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
4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,poly-cis-undecaprenyl phosphate + lipid IVA
lipid IIA + di-trans,poly-cis-undecaprenyl phosphate
show the reaction diagram
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the reaction is part of a enzymatic pathway by which Gram-negative bacteria acquire antibiotic resistance
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-
?
4-amino-4-deoxy-alpha-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[4-P-L-Ara4N]-lipid A + ditrans,octacis-undecaprenyl phosphate
show the reaction diagram
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-
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?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
LpxT-dependent lipid A modification is not restored in arnT or eptA mutants
physiological function
PmrA controls synthesis of both ArnT and EptA
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
colistin-resistant Escherichia coli isolates display significantly increased mRNA levels for the enzyme gene
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Trent, M.S.; Ribeiro, A.A.; Doerrler, W.T.; Lin, S.; Cotter, R.J.; Raetz, C.R.
Accumulation of a polyisoprene-linked amino sugar in polymyxin-resistant Salmonella typhimurium and Escherichia coli: structural characterization and transfer to lipid A in the periplasm
J. Biol. Chem.
276
43132-43144
2001
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Herrera, C.M.; Hankins, J.V.; Trent, M.S.
Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A promoting resistance to antimicrobial peptides
Mol. Microbiol.
76
1444-1460
2010
Escherichia coli (P76473)
Manually annotated by BRENDA team
Sato, T.; Shiraishi, T.; Hiyama, Y.; Honda, H.; Shinagawa, M.; Usui, M.; Kuronuma, K.; Masumori, N.; Takahashi, S.; Tamura, Y.; Yokota, S.I.
Contribution of novel amino acid alterations in PmrA or PmrB to colistin resistance in mcr-negative Escherichia coli clinical isolates, including major multidrug-resistant lineages O25b H4-ST131-H30Rx and Non-x
Antimicrob. Agents Chemother.
62
e00864-18
2018
Escherichia coli
Manually annotated by BRENDA team