AC   MF_00277;
DC   Protein; auto
TR   HAMAP; MF_00277; -; 1; level=0
XX
Names: PII_uridylyl_transf
XX
ID   GLND
DE   RecName: Full=Bifunctional uridylyltransferase/uridylyl-removing enzyme;
DE            Short=UTase/UR;
DE   AltName: Full=Bifunctional nitrogen sensor protein;
DE   AltName: Full=Bifunctional [protein-PII] modification enzyme;
DE   Includes:
DE     RecName: Full=[Protein-PII] uridylyltransferase;
DE              Short=PII uridylyltransferase;
DE              Short=UTase;
DE              EC=2.7.7.59;
DE   Includes:
DE     RecName: Full=[Protein-PII]-UMP uridylyl-removing enzyme;
DE              Short=UR;
DE              EC=3.1.4.-;
GN   Name=glnD;
XX
case defined <Property:NITROGEN_FIXATION> and <Property:NITROGEN_FIXATION>
CC   -!- FUNCTION: Modifies, by uridylylation and deuridylylation, the PII
CC       regulatory proteins (GlnB and homologs), in response to the nitrogen
CC       status of the cell that GlnD senses through the glutamine level. Under
CC       low glutamine levels, catalyzes the conversion of the PII proteins and
CC       UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD
CC       hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls
CC       uridylylation state and activity of the PII proteins, and plays an
CC       important role in the regulation of nitrogen fixation and metabolism.
else case defined <Property:NITROGEN_FIXATION> and not <Property:NITROGEN_FIXATION>
CC   -!- FUNCTION: Modifies, by uridylylation and deuridylylation, the PII
CC       regulatory proteins (GlnB and homologs), in response to the nitrogen
CC       status of the cell that GlnD senses through the glutamine level. Under
CC       low glutamine levels, catalyzes the conversion of the PII proteins and
CC       UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD
CC       hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls
CC       uridylylation state and activity of the PII proteins, and plays an
CC       important role in the regulation of nitrogen assimilation and
CC       metabolism.
else
CC   -!- FUNCTION: Modifies, by uridylylation and deuridylylation, the PII
CC       regulatory proteins (GlnB and homologs), in response to the nitrogen
CC       status of the cell that GlnD senses through the glutamine level. Under
CC       low glutamine levels, catalyzes the conversion of the PII proteins and
CC       UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD
CC       hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls
CC       uridylylation state and activity of the PII proteins, and plays an
CC       important role in the regulation of nitrogen metabolism.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-
CC         tyrosine + diphosphate; Xref=Rhea:RHEA:13673, Rhea:RHEA-COMP:12147,
CC         Rhea:RHEA-COMP:12148, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC         ChEBI:CHEBI:46858, ChEBI:CHEBI:90602; EC=2.7.7.59;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein-PII]-uridylyl-L-tyrosine + H2O = [protein-PII]-L-
CC         tyrosine + H(+) + UMP; Xref=Rhea:RHEA:48600, Rhea:RHEA-COMP:12147,
CC         Rhea:RHEA-COMP:12148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:46858, ChEBI:CHEBI:57865, ChEBI:CHEBI:90602;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- ACTIVITY REGULATION: Uridylyltransferase (UTase) activity is inhibited
CC       by glutamine, while glutamine activates uridylyl-removing (UR)
CC       activity.
CC   -!- DOMAIN: Has four distinct domains: an N-terminal nucleotidyltransferase
CC       (NT) domain responsible for UTase activity, a central HD domain that
CC       encodes UR activity, and two C-terminal ACT domains that seem to have a
CC       role in glutamine sensing.
CC   -!- SIMILARITY: Belongs to the GlnD family.
XX
DR   PROSITE; PS51671; ACT; 1; trigger=yes
DR   Pfam; PF01842; ACT; 1; trigger=no
DR   Pfam; PF01966; HD; 1; trigger=no
DR   Pfam; PF01909; NTP_transf_2; 1; trigger=no
DR   PIRSF; PIRSF006288; PII_uridyltransf; 1; trigger=no
DR   NCBIfam; TIGR01693; UTase_glnD; 1; trigger=no
DR   PROSITE; PS51831; HD; 1; trigger=yes
XX
KW   Hydrolase
KW   Magnesium
KW   Multifunctional enzyme
KW   Nucleotidyltransferase
KW   Transferase
case <Property:NITROGEN_FIXATION>
KW   Nitrogen fixation
end case
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GO   GO:0008773; F:[protein-PII] uridylyltransferase activity
GO   GO:0008081; F:phosphoric diester hydrolase activity
GO   GO:0006808; P:regulation of nitrogen utilization
case <Property:NITROGEN_FIXATION>
GO   GO:0009399; P:nitrogen fixation
end case
XX
FT   From: GLND_ECOLI (P27249)
FT   REGION          Nter..349
FT                   /note="Uridylyltransferase"
FT   REGION          350..708
FT                   /note="Uridylyl-removing"
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Size: 808-949;
Related: None;
Template: P27249; Q8RQD1; P36223; P9WN29; P41393; Q9RAE4;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: Divergent CORGL not shown in alignment and not used in size range
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# Revision 1.31 2023/06/01
//