Q1R415 · RHAB_ECOUT
- ProteinRhamnulokinase
- GenerhaB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids489 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). It could also play a role in the metabolism of some rare sugars such as L-fructose. Catalyzes the transfer of the gamma-phosphate group from ATP to the 1-hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate. It can also phosphorylate L-fuculose and L-xylulose. It requires the R-configuration at the C-3 atom.
Catalytic activity
- ATP + L-rhamnulose = ADP + H+ + L-rhamnulose 1-phosphate
Cofactor
Pathway
Carbohydrate degradation; L-rhamnose degradation; glycerone phosphate from L-rhamnose: step 2/3.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 13-17 | ATP (UniProtKB | ChEBI) | ||||
Sequence: ASSGR | ||||||
Binding site | 83 | substrate | ||||
Sequence: G | ||||||
Binding site | 236-238 | substrate | ||||
Sequence: HDT | ||||||
Active site | 237 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 259 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 296 | substrate | ||||
Sequence: N | ||||||
Binding site | 304 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 402 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | rhamnulokinase activity | |
Biological Process | rhamnose catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRhamnulokinase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionQ1R415
Proteomes
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000297519 | 1-489 | Rhamnulokinase | |||
Sequence: MTFRNCVAVDLGASSGRVMLARYERECRSLTLREIHRFNNGLHSQNGYVTWNVDSLESAIRLGLNKVCEEGIRIDSIGIDTWGVDFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTIYQLRALTEQQPELIPHIAHALLIPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHWICPQGNEIPVVAVASHDTASAVIASPLNGSRAAYLSSGTWSLMGFESQTPFTNDTALAANITNEGGAEGRYRVLKNIMGLWLLQRVLQERQINDLPALIAATQALPACRFIINPNDDRFINPDEMCSEIQAACRETAQPIPESDAELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVGGGCQNTLLNQLCADACGIRVIAGPVEASTLGNIGIQLMTLDELNNVDDFRQVVSTTANLTTFTPNPDSEIAHYVAQIHSTRQTKELCA | ||||||
Disulfide bond | 68↔222 | |||||
Sequence: CEEGIRIDSIGIDTWGVDFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTIYQLRALTEQQPELIPHIAHALLIPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHWIC | ||||||
Disulfide bond | 353↔370 | |||||
Sequence: CRETAQPIPESDAELARC | ||||||
Disulfide bond | 413↔417 | |||||
Sequence: CADAC |
Keywords
- PTM
Interaction
Subunit
Monomer.
Structure
Sequence
- Sequence statusComplete
- Length489
- Mass (Da)54,076
- Last updated2006-05-16 v1
- ChecksumE2B573E7AE58CA24
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000243 EMBL· GenBank· DDBJ | ABE09899.1 EMBL· GenBank· DDBJ | Genomic DNA |