A0A6C8LT23 · A0A6C8LT23_SALET

Function

function

Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.

Caution

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

Catalytic activity

Activity regulation

Allosterically activated by fructose-1,6-bisphosphate (F16BP) and inhibited by AMP.

Pathway

Glycan biosynthesis; glycogen biosynthesis.

Features

Showing features for binding site, site.

Type
IDPosition(s)Description
Binding site39beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI)
Binding site40AMP (UniProtKB | ChEBI)
Binding site46AMP (UniProtKB | ChEBI)
Binding site52AMP (UniProtKB | ChEBI)
Site74Could play a key role in the communication between the regulatory and the substrate sites
Site113Could play a key role in the communication between the regulatory and the substrate sites
Binding site114alpha-D-glucose 1-phosphate (UniProtKB | ChEBI)
Binding site130AMP (UniProtKB | ChEBI)
Binding site179alpha-D-glucose 1-phosphate (UniProtKB | ChEBI)
Binding site194-195alpha-D-glucose 1-phosphate (UniProtKB | ChEBI)
Binding site212alpha-D-glucose 1-phosphate (UniProtKB | ChEBI)
Binding site370AMP (UniProtKB | ChEBI)
Binding site386AMP (UniProtKB | ChEBI)
Binding site419-423beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functionglucose-1-phosphate adenylyltransferase activity
Biological Processglycogen biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glucose-1-phosphate adenylyltransferase
  • EC number
  • Alternative names
    • ADP-glucose pyrophosphorylase
      (ADPGlc PPase
      )
    • ADP-glucose synthase

Gene names

    • Name
      glgC
    • ORF names
      E4977_12540

Organism names

Accessions

  • Primary accession
    A0A6C8LT23

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain22-291Nucleotidyl transferase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    431
  • Mass (Da)
    48,446
  • Last updated
    2020-06-17 v1
  • Checksum
    12ECFEFE40C913AB
MVSLEKNDRVMLARQLPLKSVALILAGGRGTRLKDLTNKRAKPAVHFGGKFRIIDFALSNCLNSGIRRIGVITQYQSHTLVQHIQRGWSLFSEEMNEFVDLLPAQQRMKGENWYRGTADAVTQNLDIIRRYKAEYVVILAGDHIYKQDYSRMLIDHVEKGARCTVACMPVPIKEATAFGVMAVDESDKIIDFVEKPANPPAMPGDASKALASMGIYVFDADYLYELLAADDKDDASSHDFGKDIIPKITREGMAYAHPFPLSCVQSDPQAEPYWRDVGTLEAYWKANLDLASVTPELDMYDQNWPIRTHMESLPPAKFVQDRSGSHGMTLNSLVSGGCIISGSVVVQSVLFPRVRINSFCNIDSAVLLPEVWVGRSCRLRRCVIDRACIIPEGMVIGENAEEDARRFYRSEEGIVLVTREMLRKLQVKQER

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SRDL01000006
EMBL· GenBank· DDBJ
KAA6960962.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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