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Protein

L-Rhamnulokinase

Gene

rhaB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 Publications

Catalytic activityi

ATP + L-rhamnulose = ADP + L-rhamnulose 1-phosphate.UniRule annotation2 Publications

Cofactori

Mg2+UniRule annotation1 PublicationNote: It can also use manganese, cobalt, iron, calcium and copper ions.1 Publication

Kineticsi

  1. KM=82 µM for L-rhamnulose (at pH 8.5 and 37 degrees Celsius)1 Publication
  2. KM=110 µM for ATP (at pH 8.5 and 37 degrees Celsius)1 Publication
  3. KM=270 µM for magnesium ion (at pH 8.5 and 37 degrees Celsius)1 Publication
  4. KM=3 mM for beta-L-fructose (at pH 8)1 Publication

    pH dependencei

    Optimum pH is 8.5.1 Publication

    Pathwayi: L-rhamnose degradation

    This protein is involved in step 2 of the subpathway that synthesizes glycerone phosphate from L-rhamnose.UniRule annotation
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. L-rhamnose isomerase (rhaA)
    2. L-Rhamnulokinase (rhaB)
    3. Rhamnulose-1-phosphate aldolase (rhaD)
    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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei83 – 831Substrate; via amide nitrogen and carbonyl oxygenUniRule annotation1 Publication
    Active sitei237 – 2371Proton acceptorUniRule annotation1 Publication
    Binding sitei259 – 2591ATPUniRule annotation1 Publication
    Binding sitei296 – 2961SubstrateUniRule annotation1 Publication
    Binding sitei304 – 3041ATPUniRule annotation1 Publication
    Binding sitei402 – 4021ATP; via amide nitrogenUniRule annotation1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi13 – 175ATPUniRule annotation1 Publication

    GO - Molecular functioni

    • ATP binding Source: UniProtKB
    • rhamnulokinase activity Source: UniProtKB

    GO - Biological processi

    • rhamnose catabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Rhamnose metabolism

    Keywords - Ligandi

    ATP-binding, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:RHAMNULOKIN-MONOMER.
    ECOL316407:JW3875-MONOMER.
    MetaCyc:RHAMNULOKIN-MONOMER.
    BRENDAi2.7.1.5. 2026.
    UniPathwayiUPA00541; 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
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11868. rhaB.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene are unable to utilize rhamnose as a source of carbon.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi69 – 691E → A: Same kinase activity as the wild-type; when associated with A-70 and A-73. 1 Publication
    Mutagenesisi70 – 701E → A: Same kinase activity as the wild-type; when associated with A-69 and A-73. 1 Publication
    Mutagenesisi73 – 731R → A: Same kinase activity as the wild-type; when associated with A-69 and A-70. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 489489L-RhamnulokinasePRO_0000090531Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi68 ↔ 222UniRule annotation1 Publication
    Disulfide bondi353 ↔ 370UniRule annotation1 Publication
    Disulfide bondi413 ↔ 417UniRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP32171.
    PRIDEiP32171.

    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 Publication

    Protein-protein interaction databases

    IntActiP32171. 2 interactions.
    STRINGi511145.b3904.

    Structurei

    Secondary structure

    1
    489
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 118Combined sources
    Beta strandi13 – 2412Combined sources
    Turni25 – 284Combined sources
    Beta strandi29 – 3911Combined sources
    Beta strandi43 – 453Combined sources
    Beta strandi48 – 503Combined sources
    Helixi53 – 6917Combined sources
    Beta strandi74 – 818Combined sources
    Beta strandi86 – 894Combined sources
    Beta strandi91 – 933Combined sources
    Beta strandi95 – 973Combined sources
    Helixi105 – 1073Combined sources
    Helixi110 – 1189Combined sources
    Helixi120 – 1278Combined sources
    Helixi136 – 14611Combined sources
    Helixi148 – 1536Combined sources
    Beta strandi156 – 1594Combined sources
    Helixi160 – 16910Combined sources
    Helixi176 – 1794Combined sources
    Helixi180 – 1823Combined sources
    Turni187 – 1893Combined sources
    Beta strandi190 – 1923Combined sources
    Helixi194 – 2007Combined sources
    Helixi204 – 2063Combined sources
    Beta strandi216 – 2216Combined sources
    Beta strandi223 – 2253Combined sources
    Beta strandi227 – 2315Combined sources
    Helixi237 – 2448Combined sources
    Beta strandi252 – 26918Combined sources
    Helixi274 – 2796Combined sources
    Beta strandi282 – 2843Combined sources
    Helixi287 – 2893Combined sources
    Beta strandi291 – 2977Combined sources
    Helixi301 – 3099Combined sources
    Helixi315 – 3228Combined sources
    Beta strandi327 – 3304Combined sources
    Helixi337 – 3393Combined sources
    Helixi345 – 35511Combined sources
    Helixi364 – 39027Combined sources
    Beta strandi395 – 4017Combined sources
    Helixi402 – 4054Combined sources
    Helixi407 – 41711Combined sources
    Beta strandi419 – 4235Combined sources
    Helixi428 – 44013Combined sources
    Helixi447 – 4559Combined sources
    Beta strandi461 – 4633Combined sources
    Helixi470 – 47910Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CGJX-ray2.26A1-489[»]
    2CGKX-ray2.46A/B1-489[»]
    2CGLX-ray1.88A1-489[»]
    ProteinModelPortaliP32171.
    SMRiP32171. Positions 2-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32171.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni236 – 2383Substrate bindingUniRule annotation1 Publication

    Sequence similaritiesi

    Belongs to the rhamnulokinase family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105DET. Bacteria.
    COG1070. LUCA.
    HOGENOMiHOG000250110.
    InParanoidiP32171.
    KOiK00848.
    OMAiHETREWT.
    PhylomeDBiP32171.

    Family and domain databases

    HAMAPiMF_01535. Rhamnulokinase. 1 hit.
    InterProiIPR018485. Carb_kinase_FGGY_C.
    IPR018484. Carb_kinase_FGGY_N.
    IPR013449. Rhamnulokinase.
    [Graphical view]
    PfamiPF02782. FGGY_C. 1 hit.
    PF00370. FGGY_N. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02627. rhamnulo_kin. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P32171-1 [UniParc]FASTAAdd to basket

    « Hide

            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
    Length:489
    Mass (Da):54,069
    Last modified:October 1, 1993 - v1
    Checksum:iAF66259EACAC5F4E
    GO

    Sequence cautioni

    The sequence CAA43001 differs from that shown. Reason: Frameshift at position 398. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti214 – 2141Missing in CAA43001 (PubMed:8396120).Curated
    Sequence conflicti388 – 3892QL → HV in CAA43001 (PubMed:8396120).Curated

    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.
    PIRiS40848.
    RefSeqiNP_418340.1. NC_000913.3.
    WP_000144073.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76886; AAC76886; b3904.
    BAE77405; BAE77405; BAE77405.
    GeneIDi948399.
    KEGGiecj:JW3875.
    eco:b3904.
    PATRICi32123317. VBIEscCol129921_4019.

    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.
    PIRiS40848.
    RefSeqiNP_418340.1. NC_000913.3.
    WP_000144073.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CGJX-ray2.26A1-489[»]
    2CGKX-ray2.46A/B1-489[»]
    2CGLX-ray1.88A1-489[»]
    ProteinModelPortaliP32171.
    SMRiP32171. Positions 2-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP32171. 2 interactions.
    STRINGi511145.b3904.

    Proteomic databases

    PaxDbiP32171.
    PRIDEiP32171.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76886; AAC76886; b3904.
    BAE77405; BAE77405; BAE77405.
    GeneIDi948399.
    KEGGiecj:JW3875.
    eco:b3904.
    PATRICi32123317. VBIEscCol129921_4019.

    Organism-specific databases

    EchoBASEiEB1814.
    EcoGeneiEG11868. rhaB.

    Phylogenomic databases

    eggNOGiENOG4105DET. Bacteria.
    COG1070. LUCA.
    HOGENOMiHOG000250110.
    InParanoidiP32171.
    KOiK00848.
    OMAiHETREWT.
    PhylomeDBiP32171.

    Enzyme and pathway databases

    UniPathwayiUPA00541; UER00602.
    BioCyciEcoCyc:RHAMNULOKIN-MONOMER.
    ECOL316407:JW3875-MONOMER.
    MetaCyc:RHAMNULOKIN-MONOMER.
    BRENDAi2.7.1.5. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP32171.
    PROiP32171.

    Family and domain databases

    HAMAPiMF_01535. Rhamnulokinase. 1 hit.
    InterProiIPR018485. Carb_kinase_FGGY_C.
    IPR018484. Carb_kinase_FGGY_N.
    IPR013449. Rhamnulokinase.
    [Graphical view]
    PfamiPF02782. FGGY_C. 1 hit.
    PF00370. FGGY_N. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02627. rhamnulo_kin. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiRHAB_ECOLI
    AccessioniPrimary (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: September 7, 2016
    This is version 120 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.