A0A9X3YXU8 · A0A9X3YXU8_9XANT
- ProteinBifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme
- GeneglnE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids938 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell.
Catalytic activity
- [glutamine synthetase]-L-tyrosine + ATP = [glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine + diphosphate
Cofactor
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | [glutamate-ammonia-ligase] adenylyltransferase activity | |
Molecular Function | ATP binding | |
Molecular Function | ligase activity | |
Molecular Function | magnesium ion binding | |
Biological Process | regulation of glutamine family amino acid metabolic process |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameBifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme
- Alternative names
Including 2 domains:
- Recommended nameGlutamine synthetase adenylyl-L-tyrosine phosphorylase
- EC number
- Alternative names
- Recommended nameGlutamine synthetase adenylyl transferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Lysobacterales > Lysobacteraceae > Xanthomonas
Accessions
- Primary accessionA0A9X3YXU8
Proteomes
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-438 | Adenylyl removase | ||||
Sequence: MSPPIVSVSPALTALIERAVARVRHALPADQSWPGDDVDQRLEKVALASEFALDTLARQPALLQHLAQPDPPPLPLPLLDPAQPQAWPAQLRRYRSAESTRLVWRDVLELDSVDDTLAGATRLAETCLQCGLQALEQQFRDRHGQVLAEDGSVQRLVVFGLGKLGGGELNFSSDVDLVYAYPQSGQSDGARPLAAEEYFARLGQQLAKLLDETTADGFSHRVDLRLRPFGTAGRVALSFTGMDHYFQREGRDWERYAWLKARAVAGDIAAGEAWLETLRPFVYRRYLDFTALDGLRDMKAAITAEVARHDRLDDIKRGPGGIREIEFLAQSLQLIRGGREPTLRERRLLPALRALVAAGQMDADNGDALIEAYRFLRRLENRLQMLRDAQTHALPQAALDRERIALGLGYADWSALLQALAPQRARVAAEFAELLAPR | ||||||
Domain | 40-274 | Glutamate-ammonia ligase adenylyltransferase repeated | ||||
Sequence: QRLEKVALASEFALDTLARQPALLQHLAQPDPPPLPLPLLDPAQPQAWPAQLRRYRSAESTRLVWRDVLELDSVDDTLAGATRLAETCLQCGLQALEQQFRDRHGQVLAEDGSVQRLVVFGLGKLGGGELNFSSDVDLVYAYPQSGQSDGARPLAAEEYFARLGQQLAKLLDETTADGFSHRVDLRLRPFGTAGRVALSFTGMDHYFQREGRDWERYAWLKARAVAGDIAAGEAW | ||||||
Domain | 296-435 | PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase | ||||
Sequence: RDMKAAITAEVARHDRLDDIKRGPGGIREIEFLAQSLQLIRGGREPTLRERRLLPALRALVAAGQMDADNGDALIEAYRFLRRLENRLQMLRDAQTHALPQAALDRERIALGLGYADWSALLQALAPQRARVAAEFAELL | ||||||
Region | 448-938 | Adenylyl transferase | ||||
Sequence: ADYWRALPEGDAAPLAGIGLHDPAGAHQVLADFAQSSGVRALSDTAGARLDRVMPALLHAATRASQPDATVRRMLGLLQATLRRTSYLALLDEQPSALARLVDVLSRSALLAERLAAHPLLLDELLDTRISGPLPDRAALHTACADTLQIDDTEAALRELNERRLALSFRIALATLDGRQQPVDSTQQLAWLAEAVVQTVLQLARRELVAAHGQVPGGAFAIIGYGSLGGLELGFGSDLDLVFLYDHPREVEASDGKRPLEAGRWFARLAQKVMTLLGAETGAGRLYDIDVRLRPDGGKGALVSSLASYRDYQRDRAWTWEHQALVRARAVAGDAALCEAFVQVRRETLTRVRDPALLHEDVRKMRARMRSELDRSDAGRLDLKQGAGGLVDLEFVLQAGVLGQAAEHPAVLLACATPALIDALVHVQWLPAESAAPLHHAHATLVEAGLSCTLDRRPRLVVSTPPIRDACQIVAAIADAQQLRFPPGKGA | ||||||
Domain | 546-788 | Glutamate-ammonia ligase adenylyltransferase repeated | ||||
Sequence: ARLVDVLSRSALLAERLAAHPLLLDELLDTRISGPLPDRAALHTACADTLQIDDTEAALRELNERRLALSFRIALATLDGRQQPVDSTQQLAWLAEAVVQTVLQLARRELVAAHGQVPGGAFAIIGYGSLGGLELGFGSDLDLVFLYDHPREVEASDGKRPLEAGRWFARLAQKVMTLLGAETGAGRLYDIDVRLRPDGGKGALVSSLASYRDYQRDRAWTWEHQALVRARAVAGDAALCEAF | ||||||
Domain | 810-893 | PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase | ||||
Sequence: RKMRARMRSELDRSDAGRLDLKQGAGGLVDLEFVLQAGVLGQAAEHPAVLLACATPALIDALVHVQWLPAESAAPLHHAHATLV |
Sequence similarities
Belongs to the GlnE family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length938
- Mass (Da)102,357
- Last updated2023-11-08 v1
- ChecksumA524157F45FD807F