A0A424YZG8 · A0A424YZG8_9BACT

  • Protein
    Bifunctional protein HldE
  • Gene
    rfaE1
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.
Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.

Catalytic activity

Pathway

Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 1/4.
Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 3/4.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site191-194ATP (UniProtKB | ChEBI)
Active site259

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionATP binding
Molecular Functionheptose 7-phosphate kinase activity
Molecular Functionheptose-1-phosphate adenylyltransferase activity
Molecular Functionphosphotransferase activity, alcohol group as acceptor
Biological ProcessADP-L-glycero-beta-D-manno-heptose biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Bifunctional protein HldE

Including 2 domains:

  • Recommended name
    D-beta-D-heptose 7-phosphate kinase
  • EC number
  • Alternative names
    • D-beta-D-heptose 7-phosphotransferase
    • D-glycero-beta-D-manno-heptose-7-phosphate kinase
  • Recommended name
    D-beta-D-heptose 1-phosphate adenylyltransferase
  • EC number
  • Alternative names
    • D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase

Gene names

    • Name
      rfaE1
    • Synonyms
      hldE
    • ORF names
      A2J15_001205
      , DZD40_06165
      , GC018_06015
      , GC019_06455

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • 54L
    • HV10
    • VIC_4/VIC
    • VIC_5/VIC
  • Taxonomic lineage
    Bacteria > Campylobacterota > Epsilonproteobacteria > Campylobacterales > Campylobacteraceae > Campylobacter

Accessions

  • Primary accession
    A0A424YZG8

Proteomes

Subcellular Location

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-309Ribokinase
Domain10-297Carbohydrate kinase PfkB
Domain334-428Cytidyltransferase-like
Region334-461Cytidylyltransferase

Sequence similarities

In the C-terminal section; belongs to the cytidylyltransferase family.
In the N-terminal section; belongs to the carbohydrate kinase PfkB family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    461
  • Mass (Da)
    51,292
  • Last updated
    2019-05-08 v1
  • Checksum
    38ADFBB65F7C6032
MLEFLSQQKPKILVVGDFMVDNYIWCDCSRVSPEAPVLVAKTLKEDKRLGGAANVYINLQSLGAEVFSLGVVGDDEGGDFLKKNLKGKFLTQKGRKTPFKNRIMARNQQVLRLDEEDISVILLENELIALFNEEIKDFTAVVLSDYAKGVLTPKVCKAMIKKANALNIPILVDPKGNDFSKYNGATLLTPNKKEALQALKFDNLEGENLEKGIKKLKDNFSLRYSIITLSEAGIAFFDESLHIVPAKALEVYDVTGAGDSVIAVLAFCLANGIEILKACEIANEAAAVVVSKIGSVSVSFDEIQSLKQMNFEKKIKNREELLKILKQNTKKVVFTNGCFDIVHFGHIKYLEKAKRLGDILVVGLNSDSSVKRLKGEKRPINSQFQRACMLAAFYFVDFVVIFEEDTPLELISFLKPDILVKGADYKDKDIIGSNLVSKVELIDFEEGFSTSNIIKQIKDKK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP031611
EMBL· GenBank· DDBJ
AXP08365.1
EMBL· GenBank· DDBJ
Genomic DNA
WHMG01000014
EMBL· GenBank· DDBJ
MPV96007.1
EMBL· GenBank· DDBJ
Genomic DNA
WHMF01000012
EMBL· GenBank· DDBJ
MPV98721.1
EMBL· GenBank· DDBJ
Genomic DNA
QURW01000015
EMBL· GenBank· DDBJ
RQD86729.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help