A0A9J6Q7I8 · A0A9J6Q7I8_9ENTR
- ProteinBifunctional protein HldE
- GenehldE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids476 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.
Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.
Catalytic activity
- ATP + D-glycero-beta-D-manno-heptose 1-phosphate + H+ = ADP-D-glycero-beta-D-manno-heptose + diphosphate
Pathway
Bacterial outer membrane biogenesis; LPS core biosynthesis.
Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 1/4.
Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 3/4.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | heptose 7-phosphate kinase activity | |
Molecular Function | heptose-1-phosphate adenylyltransferase activity | |
Molecular Function | phosphotransferase activity, alcohol group as acceptor | |
Biological Process | biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameBifunctional protein HldE
Including 2 domains:
- Recommended nameD-beta-D-heptose 7-phosphate kinase
- EC number
- Alternative names
- Recommended nameD-beta-D-heptose 1-phosphate adenylyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Silvania
Accessions
- Primary accessionA0A9J6Q7I8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-318 | Ribokinase | ||||
Sequence: MKVTLPEFERAGVMVVGDVMLDRYWYGPTSRISPEAPVPVVKVDTIEERPGGAANVAMNIASLGAHSRLVGLTGIDDAARALSKTLADVNVKCDFVSVPTHPTITKLRVLSRNQQLIRLDFEEGFEGVDPEPLHERISHALSNIGALVLSDYAKGALASVQQMIKLARDAGVPVLIDPKGTDFERYRGATLLTPNLSEFEAVAGKCKTEEEIVERGMKIIADFDFSALLVTRSEQGMTLLQPGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACYFANAAAGVVVGKLGTSTVSPIELENAVRGRADT | ||||||
Domain | 13-305 | Carbohydrate kinase PfkB | ||||
Sequence: VMVVGDVMLDRYWYGPTSRISPEAPVPVVKVDTIEERPGGAANVAMNIASLGAHSRLVGLTGIDDAARALSKTLADVNVKCDFVSVPTHPTITKLRVLSRNQQLIRLDFEEGFEGVDPEPLHERISHALSNIGALVLSDYAKGALASVQQMIKLARDAGVPVLIDPKGTDFERYRGATLLTPNLSEFEAVAGKCKTEEEIVERGMKIIADFDFSALLVTRSEQGMTLLQPGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACYFANAAAGVVVGKLGTSTVSP | ||||||
Domain | 344-469 | Cytidyltransferase-like | ||||
Sequence: MTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGETRPVNPLEQRMIVLGALEAVDWVVSFEEDTPQRLIAGILPDLLVKGGDYKPEQIAGSEEVWANGGEVMVLNFEDGCSTTNIIK | ||||||
Region | 344-476 | Cytidylyltransferase | ||||
Sequence: MTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGETRPVNPLEQRMIVLGALEAVDWVVSFEEDTPQRLIAGILPDLLVKGGDYKPEQIAGSEEVWANGGEVMVLNFEDGCSTTNIIKKIQKDNQ |
Sequence similarities
In the C-terminal section; belongs to the cytidylyltransferase family.
In the N-terminal section; belongs to the carbohydrate kinase PfkB family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length476
- Mass (Da)50,996
- Last updated2023-06-28 v1
- Checksum8B2B98EE7E9C3194