A0A0H3FL22 · A0A0H3FL22_KLEAK

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

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

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.

TypeIDPosition(s)Description
Binding site57pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site58pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site157pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site177pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Active site182Proton acceptor
Binding site235pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site271Mg2+ (UniProtKB | ChEBI)
Binding site274Mg2+ (UniProtKB | ChEBI)
Binding site276Mg2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionmetal ion binding
Molecular Functionpyridoxal phosphate binding
Molecular FunctionUDP-4-amino-4-deoxy-L-arabinose aminotransferase
Biological Processlipid A biosynthetic process
Biological Processlipopolysaccharide biosynthetic process
Biological Processresponse to antibiotic

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase
  • EC number
  • Alternative names
    • UDP-(beta-L-threo-pentapyranosyl-4''-ulose diphosphate) aminotransferase
      (UDP-Ara4O aminotransferase
      )
    • UDP-4-amino-4-deoxy-L-arabinose aminotransferase

Gene names

    • Name
      arnB
    • Ordered locus names
      EAE_05700

Organism names

Accessions

  • Primary accession
    A0A0H3FL22

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue182N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the DegT/DnrJ/EryC1 family. ArnB subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    379
  • Mass (Da)
    41,494
  • Last updated
    2015-09-16 v1
  • Checksum
    072B00570BCEC1BF
MSEFLPFSRPSMGDAELAALREVLQSGWITTGPKNQALEEAFCQLTGNRHAIAVSSATGGMHVTLMAMGIGPGDEVITPSQTWVSTLNMICLLGATPVMIDVDHDNLMITPEAVEAAITSRTKAIIPVHYAGAPADIDAIRAVGERHGIPVIEDAAHAAGTHYKGRHVGWRGTAIFSFHAIKNMTCAEGGLIVTDDDELASRIRSLKFHGLGVDAYDRQTHGRAPQAEVITPGFKYNLADINAALALVQLDKLAQANQRRAEIAQRYLRELADTPFKPLTIPAWDHQHAWHLFIIRVDEAACGISRDVLMEKLKAMGIGTGLHFRAAHTQKYYRERFPEVSLPNTEWNSARICSIPLFPDMTDDDVTRVITALHQLSGR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP002824
EMBL· GenBank· DDBJ
AEG96067.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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