A0A265B8N4 · A0A265B8N4_SALET
- ProteinBifunctional polymyxin resistance protein ArnA
- GenearnA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids660 (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 | 102 | Transition state stabilizer | ||||
Sequence: N | ||||||
Active site | 104 | Proton donor; for formyltransferase activity | ||||
Sequence: H | ||||||
Binding site | 114 | (6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 136-140 | (6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: VKRAD | ||||||
Site | 140 | Raises pKa of active site His | ||||
Sequence: D | ||||||
Binding site | 347 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 368-369 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DI | ||||||
Binding site | 393 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 398 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 432-433 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | ||||
Sequence: TS | ||||||
Active site | 434 | Proton acceptor; for decarboxylase activity | ||||
Sequence: E | ||||||
Binding site | 460 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 492 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 526-535 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | ||||
Sequence: KLIDGGQQKR | ||||||
Binding site | 613 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Active site | 619 | Proton donor; for decarboxylase activity | ||||
Sequence: R |
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
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionA0A265B8N4
Proteomes
Interaction
Subunit
Homohexamer, formed by a dimer of trimers.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-304 | Formyltransferase ArnAFT | ||||
Sequence: MKAVIFAYHDMGCQGVQAVLDAGYEIAAIFTHADNPAENTFFGSVSRLAAGLGIPVYAPDNVNHPIWIDRIAELAPDIIFSFYYRNLLSEEILHLAPAGAFNLHGSLLPAYRGRAPLNWVLVNGESETGVTLHRMVKRADAGEIVASQRVAIAQDDVALTLHHKLCQAARQLLNSILPTMKCGDIPSVPQRESDATYYGRRRPEDGLIDWHKPVSTVHNLVRAVAAPWPGAFSYNGSQKFTIWSSRICPDAQGALPGSVISVSPLRVACADGALEIITGQAGDGITVQGSQLAQTLGLVAGARL | ||||||
Domain | 57-174 | Formyl transferase N-terminal | ||||
Sequence: YAPDNVNHPIWIDRIAELAPDIIFSFYYRNLLSEEILHLAPAGAFNLHGSLLPAYRGRAPLNWVLVNGESETGVTLHRMVKRADAGEIVASQRVAIAQDDVALTLHHKLCQAARQLLN | ||||||
Domain | 203-294 | Formyl transferase C-terminal | ||||
Sequence: PEDGLIDWHKPVSTVHNLVRAVAAPWPGAFSYNGSQKFTIWSSRICPDAQGALPGSVISVSPLRVACADGALEIITGQAGDGITVQGSQLAQ | ||||||
Region | 314-660 | Dehydrogenase ArnADH | ||||
Sequence: RRIRVLILGVNGFIGNHLTERLLNEENYEVYGMDIGSNAISRFLLHPRFHFVEGDISIHSEWIEYHVKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLRIIRYCVKYRKRVVFPSTSEVYGMCTDASFDEDKSNLIVGPVNKPRWIYSVSKQLLDRVIWAYGEKEGLRFTLFRPFNWMGPRLDSLNAARIGSSRAITQLILNLVEGTPIKLIDGGQQKRCFTDIRDGIEALFRIIVNDGDRCDGKIINIGNPDNEASIQELATLLLDSFDKHPLRCHFPPFAGFQVVESRSYYGKGYQDVAHRKPSIDNARRCLGWEPSIAMRDTVEETLDFFLRSVDVAERAS | ||||||
Domain | 318-566 | NAD-dependent epimerase/dehydratase | ||||
Sequence: VLILGVNGFIGNHLTERLLNEENYEVYGMDIGSNAISRFLLHPRFHFVEGDISIHSEWIEYHVKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLRIIRYCVKYRKRVVFPSTSEVYGMCTDASFDEDKSNLIVGPVNKPRWIYSVSKQLLDRVIWAYGEKEGLRFTLFRPFNWMGPRLDSLNAARIGSSRAITQLILNLVEGTPIKLIDGGQQKRCFTDIRDGIEALFRIIVNDGDRCDGKIINIG |
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
- Length660
- Mass (Da)73,409
- Last updated2017-12-20 v1
- Checksum74989D57932AD26D
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAHMQS010000009 EMBL· GenBank· DDBJ | EBX9257352.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAAAKA010000010 EMBL· GenBank· DDBJ | HAA0834353.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAAUCN010000012 EMBL· GenBank· DDBJ | HAF1136324.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
RUBA01000029 EMBL· GenBank· DDBJ | MKI16016.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP043214 EMBL· GenBank· DDBJ | QEI78817.1 EMBL· GenBank· DDBJ | Genomic DNA |