Q0TAF9 · RHAB_ECOL5
- ProteinRhamnulokinase
- GenerhaB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids489 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). Catalyzes the transfer of the gamma-phosphate group from ATP to the 1-hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate.
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
- Short namesRhaB
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionQ0TAF9
Proteomes
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000297521 | 1-489 | Rhamnulokinase | |||
Sequence: MTFRNCVAVDLGASSGRVMLARYERECRSLTLREIHRFNNGLHSQNGYVTWNVDRLESAIRLGLNKVCEEGIRIDSIGIDTWGVDFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTIYQLRALTEQQPELIPHIAHALLIPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHWICPQGNEIPVVAVASHDTASAVIASPLNGSRAAYLSSGTWSLMGFESQTPFTNDTALAANITNEGGAEGRYRVLKNIMGLWLLQRVLQERQINDLPALIAATQALPACRFIINPNDDRFINPDEMCSEIQAACRETAQPIPESDAELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVGGGCQNALLNQLCADACGIRVIAGPVEASTLGNIGIQLMTLDELNNVDDFRQVVSTTANLTTFTPNPDSEIAHYVAQIHSTRQTKELCA | ||||||
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)54,115
- Last updated2006-09-05 v1
- Checksum02F0D88AC4AC8F7A
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000247 EMBL· GenBank· DDBJ | ABG72070.1 EMBL· GenBank· DDBJ | Genomic DNA |