B4TK42 · GLND_SALHS

Function

function

Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.

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
      SeHA_C0251

Organism names

Accessions

  • Primary accession
    B4TK42

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10001147631-890Bifunctional uridylyltransferase/uridylyl-removing enzyme

Structure

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias1-18Polar residues
Region1-21Disordered
Region1-349Uridylyltransferase
Region350-708Uridylyl-removing
Domain468-590HD
Domain709-784ACT 1
Domain816-890ACT 2

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
    890
  • Mass (Da)
    102,264
  • Last updated
    2008-09-23 v1
  • Checksum
    B4BF92D1DC4280D0
MNTLPEQHANTALPTLPDQPQNPGVWPRAELTVAGIKARIDIFQHWLGEAFDSGICAEQLIEARTEFIDQLLQRLWIEAGFGQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELLTLLWDVKLDVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLALQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTPAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNDPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPVDDEFQLRGTLIDLRDDTLFIREPQAILRMFYMMVRNSAITGIYSTTLRHLRHARRHLSQPLCYIPEARTLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRQRHPLCVDLWPRLPHPELILIAALFHDIAKGRGGDHSVLGAQDVLTFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTETRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEAALHKIWTRCRANYFVRHSPNQLAWHARHLLQHDLRQPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLAADRHDVIRTGLEQTITQRSWQPPQPRRQPAKLRHFTVETEVNFLPTHTDRKSFMELIALDQPGLLARVGQIFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQLEVQQRLTAALNPNDKG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-18Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001120
EMBL· GenBank· DDBJ
ACF66615.1
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.
FeedbackHelp