Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A2T7ANZ3 · A0A2T7ANZ3_9ENTR

  • Protein
    Bifunctional uridylyltransferase/uridylyl-removing enzyme
  • Gene
    glnD
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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 metabolism.

Caution

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

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 Functionguanosine-3',5'-bis(diphosphate) 3'-diphosphatase 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
    • ORF names
      AUN14_16865

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MOD1-Md1s
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Cronobacter

Accessions

  • Primary accession
    A0A2T7ANZ3

Proteomes

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias1-19Polar residues
Region1-23Disordered
Region1-350Uridylyltransferase
Region351-709Uridylyl-removing
Domain469-591HD
Domain710-789ACT
Domain817-891ACT

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
    891
  • Mass (Da)
    102,824
  • Last updated
    2018-07-18 v1
  • MD5 Checksum
    77AB2BDB612F4BF29BE8F4E93DBAE270
MSNTLPEQSVNTTLAPLPGQPENPATWPADALTCAQIKQHLDAFQQWLSAAFDDGFTAEQLIEARTEFIDQLLQRLWLAAGFGETPDTALVAVGGYGRGELHPLSDIDLLILSRKRLSDAQAQKVGELLTLLWDVKLEVGHSVRTLEECLLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSDGFWPSEKFFAAKVEEQNERHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLREMVGFGFLTEAERNELDECQHLLWRIRFALHLELNRYDNRLLFDRQLSVAQRLRYEGEGNEPVEHMMKDFYRVTRRVGELNQMLLQLFDEAILALTTDEKPRVLDDDFQLRGSLIDLRDETLFIREPQAILRMFYMMVRNRDITGIYSTTLRHLRHARRHLKQPLCYIPEARSLFLAMLRHPGAVSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLLKLESFAKEETRPKHPLCVELWPRLSHPELILIAALFHDIAKGRGGDHSVLGAQDILKFAELHGLNSRETQLVAWLVRHHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLICLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQSTPDMRERVRHHQLQALALLRMENIDEEALHHIWGRCRANYFVRHSPNQLAWHARHLLRHDLSQPLILLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDDMAMDTFIVLEPDGSPLSADRHEAIRHGLEQAITQRTWQPPQPRRQPAKLRHFTVDTEVNFLPTHTERKSFLELIALDQPGLLARVGQVFADLGISLHGARISTIGERVEDLFIIATADRRGLNNLLQQEVRQRLTEALNPNDKV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-19Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MSAE01000038
EMBL· GenBank· DDBJ
PUX10946.1
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