B3E6Z9 · B3E6Z9_TRIL1

Function

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Activity regulation

Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity.

GO annotations

AspectTerm
Molecular Function[protein-PII] uridylyltransferase activity
Molecular Functionphosphoric diester hydrolase activity
Biological Processregulation of nitrogen utilization

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Bifunctional uridylyltransferase/uridylyl-removing enzyme
  • Short names
    UTase/UR
  • Alternative names
    • Bifunctional [protein-PII] modification enzyme
    • Bifunctional nitrogen sensor protein

Including 2 domains:

  • Recommended name
    [Protein-PII] uridylyltransferase
  • EC number
  • Short names
    PII uridylyltransferase
    ; UTase
  • Recommended name
    [Protein-PII]-UMP uridylyl-removing enzyme
  • EC number
  • Short names
    UR

Gene names

    • Name
      glnD
    • Ordered locus names
      Glov_2691

Organism names

Accessions

  • Primary accession
    B3E6Z9

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-359Uridylyltransferase
Domain474-590HD
Domain714-799ACT
Domain827-900ACT

Domain

Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.

Sequence similarities

Belongs to the GlnD family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    900
  • Mass (Da)
    102,659
  • Last updated
    2008-07-22 v1
  • Checksum
    26B83E5B12DA177A
MPVHPISAAAIFSAGDQRSFEEQRPEILEACKQFITSSHEEIRQRHAAGASGTEVVHQLSAVMDAMVSTLFNGILGLMGADGKRLTGHLTLAAVGGYGRGELNPYSDVDIMFLHDGSVPVEAVEAFAQKLLYFLWDLRLDVGYSVRTPADCVEMAAQDTTIKTALIDCRYLAGHQPLFATLRKTVYSQILPKASDKFIKEKIAEMRRRRDKYGATIYLLEPNIKEGEGGLRDLQTALWVAQVKYKFDNPKELVIKGVLSEAELEVYHSALDHLWRMRNELHFHTRRKSDQMNFDLQVHLATFLGYKDRGKVLAVEDFMRDYYRHAARVEHFSSTLTSRCVWRDEGAAKILGYFVRRPVGNGCFVLKGELVIPDESIIDKNPAVLMQIFELAQKHGVTLNIRVKWLIRRSLHLINDKFRRNREVNQSFLNILRSEKGMADTLRLMHHLEFLNEYIPEFEHIYCKVQHDLYHIYTVDIHTLFAVEQMEKILSGELKKELPLPCAIARQIGKRELLILSILFHDIGKGEGGGHADKGADMIPTIARRMGLSKEDSERLEFLVRQHLVFAHISQRRDLTDERMIMQFARQMVTSENLKMLFLLTIADVRAVGSDVWTTWKAMLFNELYEKAFNILERGDFRLEAGTERVRSVRRKVREMVEYDIPAAVAREELRALPTRYLLSAPLQTIADHLHLLVQLNDKDLVMQVQHEQESGFSSFTICTFDTHGLFSKITGVMAANGINILGAQIFTGKNGKILDILQVNSAQGFLITDAARWQKVEADMADVLHGTVQVSDLVHRRQRPTLLPAKSARHFPTRIEIDNEVSDEYTVIDIYAHDKVGLLYLITSTINQLGLYIGVSKISTKVDQVADVFYVRDIFGHKIFAEDKLEEIRTSLSWAIDDWQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001089
EMBL· GenBank· DDBJ
ACD96404.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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