arnA fused UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronate dehydrogenase [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

Official Symbol: arnA
Official Full Name: fused UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronate dehydrogenase
Primary source: ECOCYC:G7168
Locus tag: b2255
See related: ASAP:ABE-0007460
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage: Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as: ECK2248; pmrI; SAF; yfbG
Summary: Involved in the modification of lipid A phosphates with aminoarabinose that is required for polymyxin B and cationic antimicrobial peptide resistance. [More information is available at EcoGene: EG14091]. ArnA is a bifunctional enzyme that acts within a pathway that modifies lipid A phosphates with 4-amino-4-deoxy-L-arabinose (L-Ara4N), which causes increased resistance to polymyxin . [More information is available at EcoCyc: G7168].
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NC_000913.3 Genomic Context describing neighboring genes

Go to nucleotide: Graphics FASTA GenBank

Structure of the Escherichia coli ArnA N-formyltransferase domain in complex with N(5) -formyltetrahydrofolate and UDP-Ara4N has been presented.
Title: Structure of the Escherichia coli ArnA N-formyltransferase domain in complex with N(5) -formyltetrahydrofolate and UDP-Ara4N.
the discovered conformational changes provide a mechanistic explanation for the strong cooperative effect recently reported for the ArnA dehydrogenase function.
Title: The structure of apo ArnA features an unexpected central binding pocket and provides an explanation for enzymatic cooperativity.
N-terminus verified by Edman degradation on complete protein
Title: Protein factors associated with the SsrA.SmpB tagging and ribosome rescue complex.
analysis of ArnA domains involved in 4-amino-4-deoxy-L-arabinose biosynthesis
Title: Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis.

Submit: New GeneRIF Correction

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

Function	Evidence Code	Pubs
enables NAD+ binding	IDA Inferred from Direct Assay more info	PubMed
enables UDP-4-amino-4-deoxy-L-arabinose formyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables UDP-4-amino-4-deoxy-L-arabinose formyltransferase activity	IEA Inferred from Electronic Annotation more info
enables UDP-glucuronate decarboxylase activity	IDA Inferred from Direct Assay more info	PubMed
enables UDP-glucuronic acid dehydrogenase activity	IDA Inferred from Direct Assay more info	PubMed
enables UDP-glucuronic acid dehydrogenase activity	IEA Inferred from Electronic Annotation more info
enables carboxy-lyase activity	IEA Inferred from Electronic Annotation more info
enables hydroxymethyl-, formyl- and related transferase activity	IEA Inferred from Electronic Annotation more info
enables identical protein binding	IDA Inferred from Direct Assay more info	PubMed
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables oxidoreductase activity	IEA Inferred from Electronic Annotation more info
enables oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables transferase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
acts_upstream_of_or_within UDP-4-deoxy-4-formamido-beta-L-arabinopyranose biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in UDP-D-xylose biosynthetic process	IDA Inferred from Direct Assay more info	PubMed
involved_in biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in lipid A biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in lipid A metabolic process	IEA Inferred from Electronic Annotation more info
involved_in lipopolysaccharide biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in response to antibiotic	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within response to antibiotic	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in membrane	IEA Inferred from Electronic Annotation more info
part_of protein-containing complex	IDA Inferred from Direct Assay more info	PubMed

Preferred Names: fused UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronate dehydrogenase

NP_416758.1

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