A0A2K9PGY1 · A0A2K9PGY1_9ENTR

Function

function

Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Pathway

Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 1/3.
Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 3/3.

Features

Showing features for site, active site, binding site.

TypeIDPosition(s)Description
Site102Transition state stabilizer
Active site104Proton donor; for formyltransferase activity
Binding site114(6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI)
Binding site136-140(6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI)
Site140Raises pKa of active site His
Binding site347NAD+ (UniProtKB | ChEBI)
Binding site368-369NAD+ (UniProtKB | ChEBI)
Binding site393UDP-alpha-D-glucuronate (UniProtKB | ChEBI)
Binding site398UDP-alpha-D-glucuronate (UniProtKB | ChEBI)
Binding site432-433UDP-alpha-D-glucuronate (UniProtKB | ChEBI)
Active site434Proton acceptor; for decarboxylase activity
Binding site460UDP-alpha-D-glucuronate (UniProtKB | ChEBI)
Binding site492UDP-alpha-D-glucuronate (UniProtKB | ChEBI)
Binding site526-535UDP-alpha-D-glucuronate (UniProtKB | ChEBI)
Binding site613UDP-alpha-D-glucuronate (UniProtKB | ChEBI)
Active site619Proton donor; for decarboxylase activity

GO annotations

AspectTerm
Molecular Functioncarboxy-lyase activity
Molecular FunctionUDP-4-amino-4-deoxy-L-arabinose formyltransferase activity
Molecular FunctionUDP-glucuronic acid dehydrogenase activity
Biological Processlipid A biosynthetic process
Biological Processlipopolysaccharide biosynthetic process
Biological Processresponse to antibiotic

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Bifunctional polymyxin resistance protein ArnA

Including 2 domains:

  • Recommended name
    UDP-4-amino-4-deoxy-L-arabinose formyltransferase
  • EC number
  • Alternative names
    • ArnAFT
    • UDP-L-Ara4N formyltransferase
  • Recommended name
    UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating
  • EC number
  • Alternative names
    • ArnADH
    • UDP-GlcUA decarboxylase
    • UDP-glucuronic acid dehydrogenase

Gene names

    • Name
      arnA
    • ORF names
      WM46_22285

Organism names

  • Taxonomic identifier
  • Strain
    • CFNIH2
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Citrobacter > Citrobacter freundii complex

Accessions

  • Primary accession
    A0A2K9PGY1

Proteomes

Interaction

Subunit

Homohexamer, formed by a dimer of trimers.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-304Formyltransferase ArnAFT
Domain41-176Formyl transferase N-terminal
Domain202-291Formyl transferase C-terminal
Region314-660Dehydrogenase ArnADH
Domain318-566NAD-dependent epimerase/dehydratase

Sequence similarities

In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.
In the N-terminal section; belongs to the Fmt family. UDP-L-Ara4N formyltransferase subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    660
  • Mass (Da)
    73,619
  • Last updated
    2018-04-25 v1
  • Checksum
    AC15836919DC3D4F
MKAVVFAYHDMGCSGTQALLDAGFDIAAIFTHPDVAGENHFFGSVARIAAEHGIPVYAPDDVNHPLWVDRIQKLTPDVIFSFYYRNLLCDAILSVAAKGAFNLHGSLLPAYRGRAPLNWALVNGETETGVTLHRMVRRADAGGIVAQQKVSIDADETALELHRKLCSAAQSLLRDALPTILQGTFTETAQDESKASCFGRRTPEDGRLDWNKPARQLHNLVRAVTDPWPGAYSFAGVCKFIVWKSRVRDDIPAAKPGTVVSVSPLIVSCGEQALEIVTGQTDNGLYVQGAQLALSLGLVAGALITSAPVVAIKRRTRVLILGVNGFIGNHLTERLLKDDNYEIYGLDIGSDAIGRFLSNPRFHFVEGDISIHSEWIEYHIKKCDMVLPLVAIATPIEYTRNPLRVFELDFEENLKIIRDCVKYDKRIIFPSTSEVYGMCTDNNFDEDASNLVVGPINKQRWIYSVSKQLLDRVIWAYGEKEGLRFTLFRPFNWMGPRLDNLNAARIGSSRAITQLILNLVEGSPIKLIEGGKQKRCFTDISDGIEALFRIIENKDGRCNGEIINIGNPDNEASIRELAEMLLASFERHPLRSQFPPFAGFREVESSSYYGKGYQDVEHRKPSIRNAKRCLKWTPTVKMEQTIDETLDFFLRTVELSEQAS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP025757
EMBL· GenBank· DDBJ
AUO67223.1
EMBL· GenBank· DDBJ
Genomic DNA

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