H2IT97 · H2IT97_RAHAC
- ProteinProbable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD
- GenearnD
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids299 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the deformylation of 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol to 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
Catalytic activity
- 4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + H2O = 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + formate
Pathway
Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Glycolipid biosynthesis; 4-amino-4-deoxy-alpha-L-arabinose undecaprenyl phosphate biosynthesis; 4-amino-4-deoxy-alpha-L-arabinose undecaprenyl phosphate from UDP-4-deoxy-4-formamido-beta-L-arabinose and undecaprenyl phosphate: step 2/2.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides | |
Molecular Function | hydrolase activity, acting on glycosyl bonds | |
Biological Process | 4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate biosynthetic process | |
Biological Process | lipid A biosynthetic process | |
Biological Process | lipopolysaccharide biosynthetic process | |
Biological Process | response to antibiotic | |
Biological Process | xylan catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProbable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Yersiniaceae > Rahnella
Accessions
- Primary accessionH2IT97
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-261 | NodB homology | ||||
Sequence: KKVGLRIDVDTWSGTREGVPQLLQTLANHKITASFFFSVGPDNMGRHLWRLLKPRFLWKMLRSNAASLYGWDILLAGTAWPGKLIARDLGYLMKETAKRGHEVGLHAWDHQGWQANVGKWSGEQMEEQIRLGLEALEKSLGHDVECSAVAGWRADERVIEVKERFHFYYNSDCRGTRPFLPVLENGTPGTVQIPVTLPTYDEVAGGEINADNFNDFILDAIAKDNGVPVYTIHAEVEGMSLAKQFDELLTRASAQGIQFC |
Sequence similarities
Belongs to the polysaccharide deacetylase family. ArnD deformylase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length299
- Mass (Da)33,382
- Last updated2012-03-21 v1
- ChecksumE0C1DF5351E79D90
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP003244 EMBL· GenBank· DDBJ | AEX52681.1 EMBL· GenBank· DDBJ | Genomic DNA |