A0A0J8YVP1 · A0A0J8YVP1_9GAMM
- ProteinBifunctional uridylyltransferase/uridylyl-removing enzyme
- GeneglnD
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids883 (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 metabolism.
Catalytic activity
- [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate
- [protein-PII]-uridylyl-L-tyrosine + H2O = [protein-PII]-L-tyrosine + UMP + H+
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 | guanosine-3',5'-bis(diphosphate) 3'-diphosphatase 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
Accessions
- Primary accessionA0A0J8YVP1
Proteomes
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-342 | Uridylyltransferase | ||||
Sequence: MSVPVPQALTELIHVPDSWQDNQLQRDSIKAALDHFQQRSAEAFDQGVAVDELIAARSHFIDHLLQRLWTYYQLSESTELALVAVGGYGRQELLPLSDIDLLILSRQPLTPVQAQHISELITLLWDVKLEVGQSVRTLEECLTEGLADLTIATNLIESRMLIGDVSLLLELQKNIFSEEFWPSVHFFSAKIKEQTERHLRYHGTSYNLEPDIKSSPGGLRDIHMLQWVAHRHFGATSLDNMVQFGFLTDEERDELKTCQSFLWRLRFALHQTLTRYDNRLLFDRQLSVATRLNYLGEGNTPVEKMMKDYYRVTRRIRELNTMLLQLFDEAILTLPTTERPRP | ||||||
Region | 343-701 | Uridylyl-removing | ||||
Sequence: IDDLFRLRGDLIELRDSLSFTQSPETILKMFLVMVRHPEITGIYSATLRQLRLALQQLEKPLCDIAAARPLFLEILGSSGAVSRALMPMHHHGVLAAYLPQWESIVGQMQFDLFHAYTVDEHTMRVLQKLESFGREEVRPQHPLCVEIWQRSPNHLILIIAAIFHDIAKGRGGDHSLLGAEDVHAFAKLHQLNSRDSDLIAWLVEHHLLMSVTAQRRDIQDPEVIRQFSEIMVNERQLKFLTCLTVADICATNESLWNSWKQSLLRELFFATEKQLRRGKDKRPDLRSRVRHNRQQALALLRMNDVDENRLFHLWNRCRADYFLRHTPTQLAWHAQHLLKHRLSEPLVLISPQSARGGT | ||||||
Domain | 461-576 | HD | ||||
Sequence: VDEHTMRVLQKLESFGREEVRPQHPLCVEIWQRSPNHLILIIAAIFHDIAKGRGGDHSLLGAEDVHAFAKLHQLNSRDSDLIAWLVEHHLLMSVTAQRRDIQDPEVIRQFSEIMVN | ||||||
Domain | 702-785 | ACT | ||||
Sequence: EIFIWSPDRAYLFATVAGELDRRNLSVHDAQIFTNRDGMAMDTFIVLDPEGSPLASDRHASIIQGLTQSLQQEKWIIPKTRRTS | ||||||
Domain | 809-883 | ACT | ||||
Sequence: YLELVALDQPGLLAQIGAIFAELDISLHGARISTIGERVEDLFILADNERRGLSKKMREQLRQRLTETLNPTDKI |
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
Family and domain databases
Sequence
- Sequence statusComplete
- Length883
- Mass (Da)101,978
- Last updated2015-10-14 v1
- Checksum6183BDA395B47025
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JMSP01000067 EMBL· GenBank· DDBJ | KMV73947.1 EMBL· GenBank· DDBJ | Genomic DNA |