A0A0H3FL22 · A0A0H3FL22_KLEAK
- ProteinUDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase
- GenearnB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids379 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Catalyzes the conversion of UDP-4-keto-arabinose (UDP-Ara4O) to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N). 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 + 2-oxoglutarate = UDP-beta-L-threo-pentopyranos-4-ulose + L-glutamate
Cofactor
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 2/3.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 57 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 58 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 157 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 177 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 182 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 235 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 271 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 274 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 276 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: F |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | metal ion binding | |
Molecular Function | pyridoxal phosphate binding | |
Molecular Function | UDP-4-amino-4-deoxy-L-arabinose aminotransferase | |
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 nameUDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Klebsiella/Raoultella group > Klebsiella
Accessions
- Primary accessionA0A0H3FL22
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 182 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length379
- Mass (Da)41,494
- Last updated2015-09-16 v1
- Checksum072B00570BCEC1BF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP002824 EMBL· GenBank· DDBJ | AEG96067.1 EMBL· GenBank· DDBJ | Genomic DNA |