P32171 · RHAB_ECOLI
- ProteinL-Rhamnulokinase
- GenerhaB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids489 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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. Uridine triphosphate (UTP), cytidine 5-triphosphate (CTP), guanosine 5-triphosphate (GTP), and thymidine triphosphate (TTP) also can act as phosphoryl donors. It can also phosphorylate L-fuculose and L-xylulose.
Catalytic activity
- ATP + L-rhamnulose = ADP + H+ + L-rhamnulose 1-phosphate
Cofactor
Note: It can also use manganese, cobalt, iron, calcium and copper ions.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
82 μM | L-rhamnulose | 8.5 | 37 | |||
110 μM | ATP | 8.5 | 37 | |||
270 μM | magnesium ion | 8.5 | 37 | |||
3 mM | beta-L-fructose | 8 |
pH Dependence
Optimum pH is 8.5.
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 | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | glycerol kinase activity | |
Molecular Function | rhamnulokinase activity | |
Biological Process | glycerol metabolic process | |
Biological Process | rhamnose catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameL-Rhamnulokinase
- EC number
- Short namesRhaB ; RhuK
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP32171
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Disruption phenotype
Cells lacking this gene are unable to utilize rhamnose as a source of carbon.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 69 | Same kinase activity as the wild-type; when associated with A-70 and A-73. | ||||
Sequence: E → A | ||||||
Mutagenesis | 70 | Same kinase activity as the wild-type; when associated with A-69 and A-73. | ||||
Sequence: E → A | ||||||
Mutagenesis | 73 | Same kinase activity as the wild-type; when associated with A-69 and A-70. | ||||
Sequence: R → A |
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000090531 | 1-489 | L-Rhamnulokinase | |||
Sequence: MTFRNCVAVDLGASSGRVMLARYERECRSLTLREIHRFNNGLHSQNGYVTWDVDSLESAIRLGLNKVCEEGIRIDSIGIDTWGVDFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTLYQLRALTEQQPELIPHIAHALLMPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHWICPQGNEIPVVAVASHDTASAVIASPLNGSRAAYLSSGTWSLMGFESQTPFTNDTALAANITNEGGAEGRYRVLKNIMGLWLLQRVLQEQQINDLPALISATQALPACRFIINPNDDRFINPETMCSEIQAACRETAQPIPESDAELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVGGGCQNTLLNQLCADACGIRVIAGPVEASTLGNIGIQLMTLDELNNVDDFRQVVSTTANLTTFTPNPDSEIAHYVAQIHSTRQTKELCA | ||||||
Disulfide bond | 68↔222 | |||||
Sequence: CEEGIRIDSIGIDTWGVDFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTLYQLRALTEQQPELIPHIAHALLMPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHWIC | ||||||
Disulfide bond | 353↔370 | |||||
Sequence: CRETAQPIPESDAELARC | ||||||
Disulfide bond | 413↔417 | |||||
Sequence: CADAC |
Keywords
- PTM
Proteomic databases
Expression
Induction
Induced by L-rhamnose via the RhaR-RhaS regulatory cascade. Binding of the cAMP receptor protein (CRP) is required for full expression. Also induced by L-lyxose.
Structure
Sequence
- Sequence statusComplete
- Length489
- Mass (Da)54,069
- Last updated1993-10-01 v1
- ChecksumAF66259EACAC5F4E
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 214 | in Ref. 1; CAA43001 | ||||
Sequence: Missing | ||||||
Sequence conflict | 388-389 | in Ref. 1; CAA43001 | ||||
Sequence: QL → HV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X60472 EMBL· GenBank· DDBJ | CAA43001.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
L19201 EMBL· GenBank· DDBJ | AAB03037.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC76886.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE77405.1 EMBL· GenBank· DDBJ | Genomic DNA |