HAMAP rule MF

Accession	MF_00277
Dates	1-JUN-2001 (Created) 1-JUN-2023 (Last updated, Version 31)

Name	PII_uridylyl_transf

Scope

Bacteria

Templates

P27249 (GLND_ECOLI); Q8RQD1 (GLND_AZOBR); P36223 (GLND_AZOVI); P9WN29 (GLND_MYCTU); P41393 (GLND_KLEOX); Q9RAE4 (GLND_RHILV): [Recover all]

Triggered by

HAMAP; MF_00277 (Get profile general information and statistics)

Identifier

GLND

Protein name

RecName:		Full=Bifunctional uridylyltransferase/uridylyl-removing enzyme;
		Short=UTase/UR;
AltName:		Full=Bifunctional nitrogen sensor protein;
AltName:		Full=Bifunctional [protein-PII] modification enzyme;
Includes:
	RecName:		Full=[Protein-PII] uridylyltransferase;
			Short=PII uridylyltransferase;
			Short=UTase;
			EC 2.7.7.59;
Includes:
	RecName:		Full=[Protein-PII]-UMP uridylyl-removing enzyme;
			Short=UR;
			EC 3.1.4.-;

Gene name

glnD

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 fixation and metabolism.

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.

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.

Catalytic activity	RHEA:13673: [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate EC 2.7.7.59
	RHEA:48600: [protein-PII]-uridylyl-L-tyrosine + H2O = [protein-PII]-L-tyrosine + H(+) + UMP
Cofactor	Mg(2+)
Activity regulation	Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity.
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.
Similarity	Belongs to the GlnD family.

Hydrolase
Magnesium
Multifunctional enzyme
Nucleotidyltransferase
Transferase

Nitrogen fixation

GO:0008773; Molecular function: [protein-PII] uridylyltransferase activity.
GO:0008081; Molecular function: phosphoric diester hydrolase activity.
GO:0006808; Biological process: regulation of nitrogen utilization.

GO:0009399; Biological process: nitrogen fixation.

PROSITE	PS51671; ACT; 1; trigger=PRU01007;
Pfam	PF01842; ACT; 1;
	PF01966; HD; 1;
	PF01909; NTP_transf_2; 1;
PIRSF	PIRSF006288; PII_uridyltransf; 1;
NCBIfam	TIGR01693; UTase_glnD; 1;
PROSITE	PS51831; HD; 1; trigger=PRU01175;

From: GLND_ECOLI (P27249)

Key From To Description Tag Condition FTGroup

REGION Nter 349 Uridylyltransferase

REGION 350 708 Uridylyl-removing

Size range	808-949 amino acids
Related rules	None
Fusion	None
Comments	Divergent CORGL not shown in alignment and not used in size range

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HAMAP rule MF_00277