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G2GWW7 · G2GWW7_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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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.

Type
IDPosition(s)Description
Site102Transition state stabilizer
Active site104Proton donor; for formyltransferase activity
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
      Rin_00002540

Organism names

  • Taxonomic identifier
  • Strain
    • R5.15
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > aphid secondary symbionts > Candidatus Regiella

Accessions

  • Primary accession
    G2GWW7

Proteomes

Interaction

Subunit

Homohexamer, formed by a dimer of trimers.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-304Formyltransferase ArnAFT
Domain15-173Formyl transferase N-terminal
Domain203-293Formyl transferase C-terminal
Region314-682Dehydrogenase 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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    682
  • Mass (Da)
    76,895
  • Last updated
    2011-11-16 v1
  • MD5 Checksum
    3397D67F9D0C770858289947FBD6BDD7
MKTIVFAYHNIGHAALTELATAGYDIQAVFTHLDDPQENNFFHSVAAKATEMGLPVYAPENVNHPLWVDRIKQLQPDIIFSFYYRKLLSPEILSLAPQGGFNLHGSLLPRYRGCAPVNWALVNGESETGVTLHQMLKKVDQGAIAGQRKVMIDPEDTAFTLHEKITQAAQRLLRDLLPQIKQGSITLVPQNEEEASYFGRRSAADGKIDWQQSAVTVNNLVRAVTKPYPGAFSYLGEQKLIIWQSRPLDIKHDEQPGTLLKTDPLIIACGEGALEVIAAQSDPGLYLSGKQLAQEMGMMEKGCLGIKPNSQQTKPTRVLILGVNGFIGNHLTKRLLSEDNYEIYGLDIGSDAISCFMSHPRFHFVEGDISIHSEWIEYHIKKCDVVSPLVAIATPIEYTRNPLRVFELDFEENLKIVRDCVKYKKRIVFPSTSEVYGMCDDKEFNEDSSRLIVGPINKQRWIYSVSKQLLDRVIWAYGAKEGLKFTLFRPFNWMGPRLDSLDAARIGSSRAITQLILNLVEGTPIKLIDGGEQKRCFTDIKDGIEALFRIIENRDNRCDGQIINIGNPADEASIRELAEMLVKHFEQHELYNRFPPFAGYKKIESSSHYGEGYQDVVHRTPCIKNARRLLNWQPKISMEETIKETLDFFLRSTLSHGDIAKSGEAIPTALEVAARRPGRETR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AGCA01000050
EMBL· GenBank· DDBJ
EGY29751.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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