A0A024HLW8 · A0A024HLW8_PSEKB
- ProteinBifunctional polymyxin resistance protein ArnA
- GenearnA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids669 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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.
Catalytic activity
- UDP-4-amino-4-deoxy-beta-L-arabinose + (6R)-10-formyltetrahydrofolate = UDP-4-deoxy-4-formamido-beta-L-arabinose + (6S)-5,6,7,8-tetrahydrofolate + H+
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 | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 104 | Transition state stabilizer | |||
Active site | 106 | Proton donor; for formyltransferase activity | |||
Binding site | 116 | (6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI) | |||
Binding site | 138-142 | (6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI) | |||
Site | 142 | Raises pKa of active site His | |||
Binding site | 348 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 369-370 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 394 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | |||
Binding site | 399 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | |||
Binding site | 433-434 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | |||
Active site | 435 | Proton acceptor; for decarboxylase activity | |||
Binding site | 461 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | |||
Binding site | 492 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | |||
Binding site | 526-535 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | |||
Binding site | 613 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | |||
Active site | 619 | Proton donor; for decarboxylase activity | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | carboxy-lyase activity | |
Molecular Function | UDP-4-amino-4-deoxy-L-arabinose formyltransferase activity | |
Molecular Function | UDP-glucuronic acid dehydrogenase activity | |
Biological Process | lipid A biosynthetic process | |
Biological Process | lipopolysaccharide biosynthetic process | |
Biological Process | response to antibiotic |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBifunctional polymyxin resistance protein ArnA
Including 2 domains:
- Recommended nameUDP-4-amino-4-deoxy-L-arabinose formyltransferase
- EC number
- Alternative names
- Recommended nameUDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0A024HLW8
Proteomes
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-307 | Formyltransferase ArnAFT | |||
Domain | 61-176 | Formyl transferase N-terminal | |||
Domain | 204-283 | Formyl transferase C-terminal | |||
Region | 315-669 | Dehydrogenase ArnADH | |||
Domain | 319-566 | NAD-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 statusComplete
- Length669
- Mass (Da)74,555
- Last updated2014-07-09 v1
- ChecksumFE67AB49E3A08979
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
HG322950 EMBL· GenBank· DDBJ | CDF86045.1 EMBL· GenBank· DDBJ | Genomic DNA |