B7LM76 · ARNA_ESCF3
- ProteinBifunctional polymyxin resistance protein ArnA
- GenearnA
- StatusUniProtKB reviewed (Swiss-Prot)
- 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
- NAD+ + UDP-alpha-D-glucuronate = CO2 + NADH + UDP-beta-L-threo-pentopyranos-4-ulose
Pathway
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.
Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
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: VAKAD | ||||||
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: KLIDGGKQKR | ||||||
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionB7LM76
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000137942 | 1-660 | Bifunctional polymyxin resistance protein ArnA | |||
Sequence: MKAVVFAYHDMGCLGVQALLDAGYEISAIFTHADNPAEKVFYGSVSRLAALAGIPVYAPDDINHPLWVERIAQLAPDVIFSFYYRNLLNNEILKLAPHGAFNLHGSLLPKYRGRAPLNWVLENGENETGVTLHRMVAKADAGAIIAQQRVAIDPEDAALTLHKKLCQSASQMLEYALPAIKQGQTQETAQNESEATYFGRRKPEDSFLDWNKPATVLHNMVRAVADPWPGAFSYVGTQKFTIWSSRVHPRVNAAQPGSVISVAPFLIACGDGALEVITGQSVDGITMQGSQLAQTLGLVEGSRLNSQPVCTVQRRTRVLILGVNGFIGNHLTERLLREDHYEVYGLDIGSDAISRFLTHPNFHFVEGDISIHSEWIEYHIKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLRIIRYCVQYHKRIIFPSTSEVYGMCTDKFFDEDHSNLIVGPINKPRWIYSVSKQLLDRVIWAYGEKEGLQFTLFRPFNWMGPRLDNLNAARIGSSRAITQLILNLVEGSPIKLIDGGKQKRCFTDIRDGIEALYRIIENTGNRCDGEIINIGNPDNEASIEELGKMLLASFDKHPLRQHFPPFAGFRVVESSSYYGKGYQDVEHRKPSIRNARRCLDWEPTIDMQETIDETLDFFLRTVDIVEKSS |
Interaction
Subunit
Homohexamer, formed by a dimer of trimers.
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-304 | Formyltransferase ArnAFT | ||||
Sequence: MKAVVFAYHDMGCLGVQALLDAGYEISAIFTHADNPAEKVFYGSVSRLAALAGIPVYAPDDINHPLWVERIAQLAPDVIFSFYYRNLLNNEILKLAPHGAFNLHGSLLPKYRGRAPLNWVLENGENETGVTLHRMVAKADAGAIIAQQRVAIDPEDAALTLHKKLCQSASQMLEYALPAIKQGQTQETAQNESEATYFGRRKPEDSFLDWNKPATVLHNMVRAVADPWPGAFSYVGTQKFTIWSSRVHPRVNAAQPGSVISVAPFLIACGDGALEVITGQSVDGITMQGSQLAQTLGLVEGSRL | ||||||
Region | 314-660 | Dehydrogenase ArnADH | ||||
Sequence: RRTRVLILGVNGFIGNHLTERLLREDHYEVYGLDIGSDAISRFLTHPNFHFVEGDISIHSEWIEYHIKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLRIIRYCVQYHKRIIFPSTSEVYGMCTDKFFDEDHSNLIVGPINKPRWIYSVSKQLLDRVIWAYGEKEGLQFTLFRPFNWMGPRLDNLNAARIGSSRAITQLILNLVEGSPIKLIDGGKQKRCFTDIRDGIEALYRIIENTGNRCDGEIINIGNPDNEASIEELGKMLLASFDKHPLRQHFPPFAGFRVVESSSYYGKGYQDVEHRKPSIRNARRCLDWEPTIDMQETIDETLDFFLRTVDIVEKSS |
Sequence similarities
In the N-terminal section; belongs to the Fmt family. UDP-L-Ara4N formyltransferase subfamily.
In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length660
- Mass (Da)74,249
- Last updated2009-02-10 v1
- Checksum06B402FBA1D948E9
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CU928158 EMBL· GenBank· DDBJ | CAQ88449.1 EMBL· GenBank· DDBJ | Genomic DNA |