B4TXR9 · GLND_SALSV
- ProteinBifunctional uridylyltransferase/uridylyl-removing enzyme
- GeneglnD
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids890 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 assimilation and metabolism.
Catalytic activity
- [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate
- [protein-PII]-uridylyl-L-tyrosine + H2O = [protein-PII]-L-tyrosine + H+ + UMP
Cofactor
Activity regulation
Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | [protein-PII] uridylyltransferase activity | |
Molecular Function | phosphoric diester hydrolase activity | |
Biological Process | regulation of nitrogen utilization |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameBifunctional uridylyltransferase/uridylyl-removing enzyme
- Short namesUTase/UR
- Alternative names
Including 2 domains:
- Recommended name[Protein-PII] uridylyltransferase
- EC number
- Short namesPII uridylyltransferase ; UTase
- Recommended name[Protein-PII]-UMP uridylyl-removing enzyme
- EC number
- Short namesUR
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionB4TXR9
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000114766 | 1-890 | Bifunctional uridylyltransferase/uridylyl-removing enzyme | |||
Sequence: MNTLPEQHANTALPTLPDQPQNPGVWPRAELTVAGIKARIDIFQHWLGEAFDSGICAEQLIEARTEFIDQLLQRLWIEAGFGQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELLTLLWDVKLDVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLALQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTPAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNDPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPVDDEFQLRGTLIDLRDDTLFIREPQAILRMFYMMVRNSAITGIYSTTLRHLRHARRHLSQPLCYIPEARTLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQWSLIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRQRHPLCVDLWPRLPHPELILIAALFHDIAKGRGGDHSVLGAQDVLTFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTETRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEAALHKIWTRCRANYFVRHSPNQLAWHARHLLQHDLSQPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLAADRHDVIRTGLEQTITQRSWQPPQPRRQPAKLRHFTVETEVNFLPTHTDRKSFMELIALDQPGLLARVGQIFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQLEVQQRLTAALNPNDKG |
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-18 | Polar residues | ||||
Sequence: MNTLPEQHANTALPTLPD | ||||||
Region | 1-21 | Disordered | ||||
Sequence: MNTLPEQHANTALPTLPDQPQ | ||||||
Region | 1-349 | Uridylyltransferase | ||||
Sequence: MNTLPEQHANTALPTLPDQPQNPGVWPRAELTVAGIKARIDIFQHWLGEAFDSGICAEQLIEARTEFIDQLLQRLWIEAGFGQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELLTLLWDVKLDVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLALQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTPAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNDPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRP | ||||||
Region | 350-708 | Uridylyl-removing | ||||
Sequence: VDDEFQLRGTLIDLRDDTLFIREPQAILRMFYMMVRNSAITGIYSTTLRHLRHARRHLSQPLCYIPEARTLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQWSLIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRQRHPLCVDLWPRLPHPELILIAALFHDIAKGRGGDHSVLGAQDVLTFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTETRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEAALHKIWTRCRANYFVRHSPNQLAWHARHLLQHDLSQPLVLLSPQATRGGT | ||||||
Domain | 468-590 | HD | ||||
Sequence: VDEHTIRVMLKLESFAKEETRQRHPLCVDLWPRLPHPELILIAALFHDIAKGRGGDHSVLGAQDVLTFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTETRLRFL | ||||||
Domain | 709-784 | ACT 1 | ||||
Sequence: EIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLAADRHDVIRTGLEQTITQRSWQ | ||||||
Domain | 816-890 | ACT 2 | ||||
Sequence: FMELIALDQPGLLARVGQIFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQLEVQQRLTAALNPNDKG |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length890
- Mass (Da)102,171
- Last updated2008-09-23 v1
- Checksum60AC13F1CBC6AB0D
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-18 | Polar residues | ||||
Sequence: MNTLPEQHANTALPTLPD |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001127 EMBL· GenBank· DDBJ | ACF91506.1 EMBL· GenBank· DDBJ | Genomic DNA |