A0A4S0GGB8 · A0A4S0GGB8_9HYPH

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site211-214ATP (UniProtKB | ChEBI)
Active site280

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
      EN835_010280

Organism names

Accessions

  • Primary accession
    A0A4S0GGB8

Proteomes

Subcellular Location

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-335Ribokinase
Domain53-318Carbohydrate kinase PfkB
Domain363-458Cytidyltransferase-like
Region363-496Cytidylyltransferase

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    496
  • Mass (Da)
    52,021
  • Last updated
    2019-07-31 v1
  • Checksum
    6FDABB45341E93C1
MIKQHLPSSEPLHRTIARFGEVTVLVVGDFILDRFVSGVIERISPEAPIPVLHGRGEMLAMGGAGNVVSNIVSLGGAAIPVAVIGADKAGDDLLRMLGDLGADTDGLVQRQDRMTSSKSRFSALNQQVLRFDEEEIKPLARSERAMLIEHFQAALARADIVILSDYGKGVLLDGVAAELIAICRDAGKPVLVDPKGRDYARYGGATAVTPNRKELGEAVGRAVFGDDEIVAAARDLIAAHDFEFIVATRSEKGMSVVTAEDARHISTQAREVFDVSGAGDTVIATFALSLAAGADRVQAATIANAAGGVVVGKRGTARLSVEELSGALFRSHGPVVHQDAILDATAAARMVAAWKDEGLAVGFTNGCFDILHAGHVSLLHAARSQCDRLVLGLNSDASVRRLKGPGRPVNDQHDRACVLAALASVDAVVVFEEDTPLKLIETLKPDILVKGADYTIETVVGADVVQKAGGRVVLVDLVAGKSTTNTIGKLRAGGPN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
RZOX02000007
EMBL· GenBank· DDBJ
TGR66676.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
FeedbackHelp