A0AAP1MWY2 · A0AAP1MWY2_9ENTR

  • Protein
    Bifunctional polymyxin resistance protein ArnA
  • Gene
    arnA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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
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 Functionoxidoreductase activity
Molecular Functiontransferase activity

Keywords

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
      IB240_15295

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • RLT01
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Klebsiella/Raoultella group > Raoultella

Accessions

  • Primary accession
    A0AAP1MWY2

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
Domain21-177Formyl transferase N-terminal
Domain202-294Formyl transferase C-terminal
Region314-661Dehydrogenase 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
    661
  • Mass (Da)
    73,918
  • Last updated
    2024-10-02 v1
  • Checksum
    AEDD38476FEB270F
MKAVVFAYHDMGCAGIQSLLDSGYEIAAIFTHPDNPGENHFFGSVARIAAEQGIPVWAPEDVNHPLWIERIRDMKPDVLFSFYYRNMLGDDILSLAPKGGFNLHGSLLPQYRGRAPLNWVLVNGETETGVTLHRMVSRADAGAIVAQQTVAIGADDVALTLHRKLCAAASELLNQALPAIREDKIQDRAQDESQATYVGRRTPEDGRLDWDKPALTLHNLVRAVSDPWPGAFGYVGANKFIVWKSRVRQDLAAAKPGTVMSTSPLVIACQDGALEIVTGQTERGVYMQGTQLAQALGLVSGAVLSSKPVVAIKRRTRVLILGVNGFIGNHLTERLLADDNYEIYGLDIGSDAIGRFLGNPRFHFVEGDISIHSEWIEYHIKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLKIIRDCVKYDKRIIFPSTSEVYGMCTDKNFDEDTSNLVVGPINKQRWIYSVSKQLLDRVIWAYGDKSGLRFTLFRPFNWMGPRLDNLNAARIGSSRAITQLILNLVEGSPIKLIEGGKQKRCFTDISDGIEALFRIIENKDGRCDGQIINIGNPENEASIKELAEMLLACFERHPLRNNFPPFAGFRDVESSDYYGKGYQDVEHRKPSIRNAKRCLNWTPTVPMEETVEHTLDFFLRTVELVDDKTS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACVBV010000004
EMBL· GenBank· DDBJ
MBD9719767.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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