Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_00277
    • taxon = Bacteria
    • fragment ≠ the sequence is fragmented

Special conditions

    • proteome property = NITROGEN_FIXATION=Yes
    • proteome property = NITROGEN_FIXATION=No
    • proteome property ≠ NITROGEN_FIXATION=*
    • Subsequence at position 350 - 708 aligns to entry P27249 (individually applies "Uridylyl-removing")
    • Subsequence at position @NTER|+1@ - 349 aligns to entry P27249 (individually applies "Uridylyltransferase")

... then these annotations are applied i

Protein namei

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

Cleaved chain(s) or included domain(s)i

  • Includes domain:
    Recommended name:
    [Protein-PII]-UMP uridylyl-removing enzyme (EC:3.1.4.-)
    Short name:
    UR
  • Includes domain:
    Recommended name:
    [Protein-PII] uridylyltransferase (EC:2.7.7.59)
    Short name:
    PII uridylyltransferase
    Short name:
    UTase

Gene namei

  • Name:glnD

Enzyme regulationi

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

Functioni

  • 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 fixation and metabolism.
  • 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.
  • 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.

Cofactori

Domaini

  • 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 similaritiesi

Catalytic activityi

  • UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII].
  • Uridylyl-[protein-PII] + H2O = UMP + [protein-PII].

Regioni

  • Uridylyl-removing (to residues corresponding to positions 350 - 708)
  • Uridylyltransferase (to residues corresponding to positions @NTER|+1@i - 349)

Keywordsi

GO (Gene Ontology) termsi