J3H6M3 · J3H6M3_9PSED

  • Protein
    Bifunctional polymyxin resistance protein ArnA
  • Gene
    arnA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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
Site104Transition state stabilizer
Active site106Proton donor; for formyltransferase activity
Binding site116(6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI)
Binding site138-142(6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI)
Site142Raises pKa of active site His
Binding site350NAD+ (UniProtKB | ChEBI)
Binding site371-372NAD+ (UniProtKB | ChEBI)
Binding site396UDP-alpha-D-glucuronate (UniProtKB | ChEBI)
Binding site401UDP-alpha-D-glucuronate (UniProtKB | ChEBI)
Binding site435-436UDP-alpha-D-glucuronate (UniProtKB | ChEBI)
Active site437Proton acceptor; for decarboxylase activity
Binding site463UDP-alpha-D-glucuronate (UniProtKB | ChEBI)
Binding site494UDP-alpha-D-glucuronate (UniProtKB | ChEBI)
Binding site528-537UDP-alpha-D-glucuronate (UniProtKB | ChEBI)
Binding site615UDP-alpha-D-glucuronate (UniProtKB | ChEBI)
Active site621Proton 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
      PMI34_04032

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • GM74
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    J3H6M3

Proteomes

Interaction

Subunit

Homohexamer, formed by a dimer of trimers.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-307Formyltransferase ArnAFT
Domain27-176Formyl transferase N-terminal
Domain204-284Formyl transferase C-terminal
Region317-663Dehydrogenase ArnADH
Domain321-568NAD-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
    663
  • Mass (Da)
    73,669
  • Last updated
    2012-10-03 v1
  • Checksum
    F17F758070023874
MSAKAVVFAYHDIGCAGIESLLCSGFEIAAVFTHADDPKENAFYGSVAQLCARHGIAVHAPEDANHPLWIERIAKLDPDYIFSFYYRNLLGEPLLATARKGAFNLHGSLLPRYRGRAPANWVLVNGETETGVTLHRMVKRADAGAIVAQQKVAIERSDTALSLHAKLRTAASDLLRDTLPALLQGKASETPQDESRATVFGRRTPADGKLVWAKPAEELFNLVRAVTQPYPGAFCAVGEHKLIVWSAEVAKGNEGLAPGCVISVDPLRIACGQDSLVINAGQRNDNGLYLSGPQLANELGLVDGSVLRGAESGRAPRRTRVLILGVNGFIGNHLSERLLSDDRYEVYGLDIGSDAIERLRSHPNFHFVEGDISIHSEWIEYHIKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLKLVRYCVKYNKRVIFPSTSEVYGMCQDPNFDEDNSNLVVGPINKQRWIYSVSKQLLDRVIWAYGQKGLNFTLFRPFNWMGPRLDRLDSARIGSSRAITQLILNLVEGTPIRLFDGGEQKRCFTDIADGVEALARIIDNDNDVCNGQIINIGNPDNEASIRQLGEELLRQFEAHPLRANFPPFAGFRDIESKAFYGTGYQDVSHRKPSIANAKRLLDWTPTVEMSETIGNTLDFFLREAMLEIADKR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AKJG01000106
EMBL· GenBank· DDBJ
EJM86135.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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