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UniProtKB - P32171 (RHAB_ECOLI)
Protein
L-Rhamnulokinase
Gene
rhaB
Organism
Escherichia coli (strain K12)
Status
Functioni
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.
UniRule annotation3 PublicationsCatalytic activityi
- EC:2.7.1.5UniRule annotation2 Publications
Cofactori
Mg2+UniRule annotation1 PublicationNote: It can also use manganese, cobalt, iron, calcium and copper ions.1 Publication
Kineticsi
- KM=82 µM for L-rhamnulose (at pH 8.5 and 37 degrees Celsius)1 Publication
- KM=110 µM for ATP (at pH 8.5 and 37 degrees Celsius)1 Publication
- KM=270 µM for magnesium ion (at pH 8.5 and 37 degrees Celsius)1 Publication
- KM=3 mM for beta-L-fructose (at pH 8)1 Publication
pH dependencei
Optimum pH is 8.5.1 Publication
: L-rhamnose degradation Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes glycerone phosphate from L-rhamnose.UniRule annotation This subpathway is part of the pathway L-rhamnose degradation, which is itself part of Carbohydrate degradation.View all proteins of this organism that are known to be involved in the subpathway that synthesizes glycerone phosphate from L-rhamnose, the pathway L-rhamnose degradation and in Carbohydrate degradation.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 83 | Substrate; via amide nitrogen and carbonyl oxygenUniRule annotation1 Publication | 1 | |
Active sitei | 237 | Proton acceptorUniRule annotation1 Publication | 1 | |
Binding sitei | 259 | ATPUniRule annotation1 Publication | 1 | |
Binding sitei | 296 | SubstrateUniRule annotation1 Publication | 1 | |
Binding sitei | 304 | ATPUniRule annotation1 Publication | 1 | |
Binding sitei | 402 | ATP; via amide nitrogenUniRule annotation1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 13 – 17 | ATPUniRule annotation1 Publication | 5 |
GO - Molecular functioni
- ATP binding Source: UniProtKB
- rhamnulokinase activity Source: UniProtKB
GO - Biological processi
- rhamnose catabolic process Source: UniProtKB
Keywordsi
Molecular function | Kinase, Transferase |
Biological process | Rhamnose metabolism |
Ligand | ATP-binding, Magnesium, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:RHAMNULOKIN-MONOMER |
BRENDAi | 2.7.1.5, 2026 |
UniPathwayi | UPA00541;UER00602 |
Names & Taxonomyi
Protein namesi | Recommended name: L-Rhamnulokinase1 PublicationUniRule annotation (EC:2.7.1.5UniRule annotation2 Publications)Short name: RhaB1 PublicationUniRule annotation Short name: RhuK1 Publication Alternative name(s): ATP:L-rhamnulose phosphotransferase1 PublicationUniRule annotation L-rhamnulose 1-kinase1 PublicationUniRule annotation Rhamnulose kinase1 PublicationUniRule annotation |
Gene namesi | Name:rhaB1 PublicationUniRule annotation Ordered Locus Names:b3904, JW3875 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Disruption phenotypei
Cells lacking this gene are unable to utilize rhamnose as a source of carbon.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 69 | E → A: Same kinase activity as the wild-type; when associated with A-70 and A-73. 1 Publication | 1 | |
Mutagenesisi | 70 | E → A: Same kinase activity as the wild-type; when associated with A-69 and A-73. 1 Publication | 1 | |
Mutagenesisi | 73 | R → A: Same kinase activity as the wild-type; when associated with A-69 and A-70. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000090531 | 1 – 489 | L-RhamnulokinaseAdd BLAST | 489 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 68 ↔ 222 | UniRule annotation1 Publication | ||
Disulfide bondi | 353 ↔ 370 | UniRule annotation1 Publication | ||
Disulfide bondi | 413 ↔ 417 | UniRule annotation |
Keywords - PTMi
Disulfide bondProteomic databases
PaxDbi | P32171 |
PRIDEi | P32171 |
Expressioni
Inductioni
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.3 Publications
Interactioni
Subunit structurei
Monomer.
UniRule annotation1 PublicationProtein-protein interaction databases
IntActi | P32171, 2 interactors |
STRINGi | 511145.b3904 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | P32171 |
SMRi | P32171 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P32171 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 236 – 238 | Substrate bindingUniRule annotation1 Publication | 3 |
Sequence similaritiesi
Belongs to the rhamnulokinase family.UniRule annotation
Phylogenomic databases
eggNOGi | COG1070, Bacteria |
HOGENOMi | CLU_039395_0_0_6 |
InParanoidi | P32171 |
OMAi | MPDLFNY |
PhylomeDBi | P32171 |
Family and domain databases
CDDi | cd07771, FGGY_RhuK, 1 hit |
HAMAPi | MF_01535, Rhamnulokinase, 1 hit |
InterProi | View protein in InterPro IPR043129, ATPase_NBD IPR018485, Carb_kinase_FGGY_C IPR018484, Carb_kinase_FGGY_N IPR013449, Rhamnulokinase |
Pfami | View protein in Pfam PF02782, FGGY_C, 1 hit PF00370, FGGY_N, 1 hit |
SUPFAMi | SSF53067, SSF53067, 2 hits |
TIGRFAMsi | TIGR02627, rhamnulo_kin, 1 hit |
i Sequence
Sequence statusi: Complete.
P32171-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTFRNCVAVD LGASSGRVML ARYERECRSL TLREIHRFNN GLHSQNGYVT
60 70 80 90 100
WDVDSLESAI RLGLNKVCEE GIRIDSIGID TWGVDFVLLD QQGQRVGLPV
110 120 130 140 150
AYRDSRTNGL MAQAQQQLGK RDIYQRSGIQ FLPFNTLYQL RALTEQQPEL
160 170 180 190 200
IPHIAHALLM PDYFSYRLTG KMNWEYTNAT TTQLVNINSD DWDESLLAWS
210 220 230 240 250
GANKAWFGRP THPGNVIGHW ICPQGNEIPV VAVASHDTAS AVIASPLNGS
260 270 280 290 300
RAAYLSSGTW SLMGFESQTP FTNDTALAAN ITNEGGAEGR YRVLKNIMGL
310 320 330 340 350
WLLQRVLQEQ QINDLPALIS ATQALPACRF IINPNDDRFI NPETMCSEIQ
360 370 380 390 400
AACRETAQPI PESDAELARC IFDSLALLYA DVLHELAQLR GEDFSQLHIV
410 420 430 440 450
GGGCQNTLLN QLCADACGIR VIAGPVEAST LGNIGIQLMT LDELNNVDDF
460 470 480
RQVVSTTANL TTFTPNPDSE IAHYVAQIHS TRQTKELCA
Sequence cautioni
The sequence CAA43001 differs from that shown. Reason: Frameshift.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 214 | Missing in CAA43001 (PubMed:8396120).Curated | 1 | |
Sequence conflicti | 388 – 389 | QL → HV in CAA43001 (PubMed:8396120).Curated | 2 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X60472 Genomic DNA Translation: CAA43001.1 Frameshift. L19201 Genomic DNA Translation: AAB03037.1 U00096 Genomic DNA Translation: AAC76886.1 AP009048 Genomic DNA Translation: BAE77405.1 |
PIRi | S40848 |
RefSeqi | NP_418340.1, NC_000913.3 WP_000144073.1, NZ_SSZK01000014.1 |
Genome annotation databases
EnsemblBacteriai | AAC76886; AAC76886; b3904 BAE77405; BAE77405; BAE77405 |
GeneIDi | 948399 |
KEGGi | ecj:JW3875 eco:b3904 |
PATRICi | fig|1411691.4.peg.2802 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X60472 Genomic DNA Translation: CAA43001.1 Frameshift. L19201 Genomic DNA Translation: AAB03037.1 U00096 Genomic DNA Translation: AAC76886.1 AP009048 Genomic DNA Translation: BAE77405.1 |
PIRi | S40848 |
RefSeqi | NP_418340.1, NC_000913.3 WP_000144073.1, NZ_SSZK01000014.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2CGJ | X-ray | 2.26 | A | 1-489 | [»] | |
2CGK | X-ray | 2.46 | A/B | 1-489 | [»] | |
2CGL | X-ray | 1.88 | A | 1-489 | [»] | |
AlphaFoldDBi | P32171 | |||||
SMRi | P32171 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P32171, 2 interactors |
STRINGi | 511145.b3904 |
Proteomic databases
PaxDbi | P32171 |
PRIDEi | P32171 |
Genome annotation databases
EnsemblBacteriai | AAC76886; AAC76886; b3904 BAE77405; BAE77405; BAE77405 |
GeneIDi | 948399 |
KEGGi | ecj:JW3875 eco:b3904 |
PATRICi | fig|1411691.4.peg.2802 |
Organism-specific databases
EchoBASEi | EB1814 |
Phylogenomic databases
eggNOGi | COG1070, Bacteria |
HOGENOMi | CLU_039395_0_0_6 |
InParanoidi | P32171 |
OMAi | MPDLFNY |
PhylomeDBi | P32171 |
Enzyme and pathway databases
UniPathwayi | UPA00541;UER00602 |
BioCyci | EcoCyc:RHAMNULOKIN-MONOMER |
BRENDAi | 2.7.1.5, 2026 |
Miscellaneous databases
EvolutionaryTracei | P32171 |
PROi | PR:P32171 |
Family and domain databases
CDDi | cd07771, FGGY_RhuK, 1 hit |
HAMAPi | MF_01535, Rhamnulokinase, 1 hit |
InterProi | View protein in InterPro IPR043129, ATPase_NBD IPR018485, Carb_kinase_FGGY_C IPR018484, Carb_kinase_FGGY_N IPR013449, Rhamnulokinase |
Pfami | View protein in Pfam PF02782, FGGY_C, 1 hit PF00370, FGGY_N, 1 hit |
SUPFAMi | SSF53067, SSF53067, 2 hits |
TIGRFAMsi | TIGR02627, rhamnulo_kin, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | RHAB_ECOLI | |
Accessioni | P32171Primary (citable) accession number: P32171 Secondary accession number(s): Q2M8K1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1993 |
Last sequence update: | October 1, 1993 | |
Last modified: | May 25, 2022 | |
This is version 147 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families