C6DAW5 · ARNA_PECCP
- ProteinBifunctional polymyxin resistance protein ArnA
- GenearnA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids672 (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: VSRAD | ||||||
Site | 140 | Raises pKa of active site His | ||||
Sequence: D | ||||||
Binding site | 353 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 374-375 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DI | ||||||
Binding site | 399 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 404 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 438-439 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | ||||
Sequence: TS | ||||||
Active site | 440 | Proton acceptor; for decarboxylase activity | ||||
Sequence: E | ||||||
Binding site | 466 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 498 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 532-541 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | ||||
Sequence: KLVDGGAQKR | ||||||
Binding site | 619 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Active site | 625 | 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 > Pectobacteriaceae > Pectobacterium
Accessions
- Primary accessionC6DAW5
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000213730 | 1-672 | Bifunctional polymyxin resistance protein ArnA | |||
Sequence: MKAIVFAYHDIGCVGLEALKLAGYEIQAVFTHSDAPGENHFYASVAKAAAEMDVPVFAPEDVNHPLWVNRIRELAPDVIFSFYYRTLLSDDILQLPSFGAFNLHGSLLPRYRGRAPVNWVLVNGETQTGVTLHKMVSRADAGDIVAQSVVEIDDEDTALTLHGKCRTTAAALLAQQLPLIRSREIMLTPQDESQASYFGRRTAADGLIDWQKSAREINNLIRAVTEPYPGAFTFLGERKVVIWRARVLKNDSVKANGVKQEPGSIISTSPLVVSCGEDALEIVSGQSESGLYMSGSRLAAEMGMVPQAKLGNLASRVQRRRTRVLILGVNGFIGNHLTERLLRDDRYEIYGLDISSDAIARFLGDPRFHFVEGDISIHNEWIEYHIKKCDVILPLVAIATPIEYTRNPLRVFELDFEENLKIVRDCVRYNKRIVFPSTSEVYGMCDDKEFDEDTSRLIVGPINKQRWIYSVSKQLLDRVIWAYGAKNGLRFTLFRPFNWMGPRLDTLDAARIGSSRAITQLILNLVEGSPIKLVDGGAQKRCFTDIHDGIEALFRIIENRNGQCDGQIINIGNPHNEASIRELGDMLLTSFNAHPLRDRFPPFAGFIEVESSSYYGKGYQDVAHRTPSIRNAKRLLEWEPTVKMEQTVAETLDYFLRTVDPQHADNVTDTQG |
Interaction
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-310 | Formyltransferase ArnAFT | ||||
Sequence: MKAIVFAYHDIGCVGLEALKLAGYEIQAVFTHSDAPGENHFYASVAKAAAEMDVPVFAPEDVNHPLWVNRIRELAPDVIFSFYYRTLLSDDILQLPSFGAFNLHGSLLPRYRGRAPVNWVLVNGETQTGVTLHKMVSRADAGDIVAQSVVEIDDEDTALTLHGKCRTTAAALLAQQLPLIRSREIMLTPQDESQASYFGRRTAADGLIDWQKSAREINNLIRAVTEPYPGAFTFLGERKVVIWRARVLKNDSVKANGVKQEPGSIISTSPLVVSCGEDALEIVSGQSESGLYMSGSRLAAEMGMVPQAKL | ||||||
Region | 320-672 | Dehydrogenase ArnADH | ||||
Sequence: RRTRVLILGVNGFIGNHLTERLLRDDRYEIYGLDISSDAIARFLGDPRFHFVEGDISIHNEWIEYHIKKCDVILPLVAIATPIEYTRNPLRVFELDFEENLKIVRDCVRYNKRIVFPSTSEVYGMCDDKEFDEDTSRLIVGPINKQRWIYSVSKQLLDRVIWAYGAKNGLRFTLFRPFNWMGPRLDTLDAARIGSSRAITQLILNLVEGSPIKLVDGGAQKRCFTDIHDGIEALFRIIENRNGQCDGQIINIGNPHNEASIRELGDMLLTSFNAHPLRDRFPPFAGFIEVESSSYYGKGYQDVAHRTPSIRNAKRLLEWEPTVKMEQTVAETLDYFLRTVDPQHADNVTDTQG |
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
- Length672
- Mass (Da)75,416
- Last updated2009-09-01 v1
- Checksum28BE7F5CBE4EB584
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001657 EMBL· GenBank· DDBJ | ACT13949.1 EMBL· GenBank· DDBJ | Genomic DNA |