ID   RHAB_ECOLI              Reviewed;         489 AA.
AC   P32171; Q2M8K1;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   02-SEP-2026, entry version 164.
DE   RecName: Full=L-Rhamnulokinase {ECO:0000255|HAMAP-Rule:MF_01535, ECO:0000303|PubMed:8396120};
DE            Short=RhaB {ECO:0000255|HAMAP-Rule:MF_01535, ECO:0000303|PubMed:8396120};
DE            Short=RhuK {ECO:0000303|PubMed:16674975};
DE            EC=2.7.1.5 {ECO:0000255|HAMAP-Rule:MF_01535, ECO:0000269|PubMed:14264882, ECO:0000269|PubMed:16674975};
DE   AltName: Full=ATP:L-rhamnulose phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01535, ECO:0000303|PubMed:14264882};
DE   AltName: Full=L-rhamnulose 1-kinase {ECO:0000255|HAMAP-Rule:MF_01535, ECO:0000303|PubMed:16674975};
DE   AltName: Full=Rhamnulose kinase {ECO:0000255|HAMAP-Rule:MF_01535, ECO:0000303|PubMed:8396120};
GN   Name=rhaB {ECO:0000255|HAMAP-Rule:MF_01535,
GN   ECO:0000303|PubMed:8396120}; OrderedLocusNames=b3904, JW3875;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=8396120; DOI=10.1128/jb.175.17.5585-5594.1993;
RA   Moralejo P., Egan S.M., Hidalgo E.F., Aguilar J.;
RT   "Sequencing and characterization of a gene cluster encoding the enzymes for
RT   L-rhamnose metabolism in Escherichia coli.";
RL   J. Bacteriol. 175:5585-5594(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA   Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT   from 87.2 to 89.2 minutes.";
RL   Nucleic Acids Res. 21:3391-3398(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP   SPECIFICITY, AND COFACTOR.
RX   PubMed=14264882; DOI=10.1016/0926-6569(64)90009-4;
RA   Chiu T.H., Feingold D.S.;
RT   "The purification and properties of L-rhamnulokinase.";
RL   Biochim. Biophys. Acta 92:489-497(1964).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12;
RX   PubMed=5341476; DOI=10.1093/genetics/55.3.557;
RA   Power J.;
RT   "The L-rhamnose genetic system in Escherichia coli K-12.";
RL   Genetics 55:557-568(1967).
RN   [7]
RP   INDUCTION.
RC   STRAIN=K12;
RX   PubMed=1650346; DOI=10.1128/jb.173.16.5144-5150.1991;
RA   Badia J., Gimenez R., Baldoma L., Barnes E., Fessner W.D., Aguilar J.;
RT   "L-lyxose metabolism employs the L-rhamnose pathway in mutant cells of
RT   Escherichia coli adapted to grow on L-lyxose.";
RL   J. Bacteriol. 173:5144-5150(1991).
RN   [8]
RP   INDUCTION.
RC   STRAIN=ECL116;
RX   PubMed=8230210; DOI=10.1006/jmbi.1993.1565;
RA   Egan S.M., Schleif R.F.;
RT   "A regulatory cascade in the induction of rhaBAD.";
RL   J. Mol. Biol. 234:87-98(1993).
RN   [9]
RP   INDUCTION.
RX   PubMed=10852886; DOI=10.1128/jb.182.12.3529-3535.2000;
RA   Holcroft C.C., Egan S.M.;
RT   "Roles of cyclic AMP receptor protein and the carboxyl-terminal domain of
RT   the alpha subunit in transcription activation of the Escherichia coli
RT   rhaBAD operon.";
RL   J. Bacteriol. 182:3529-3535(2000).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) IN COMPLEX WITH ADP AND FRUCTOSE,
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP   GLU-69; GLU-70 AND ARG-73, ACTIVE SITE, SUBUNIT, REACTION MECHANISM, AND
RP   DISULFIDE BOND.
RX   PubMed=16674975; DOI=10.1016/j.jmb.2006.04.013;
RA   Grueninger D., Schulz G.E.;
RT   "Structure and reaction mechanism of L-rhamnulose kinase from Escherichia
RT   coli.";
RL   J. Mol. Biol. 359:787-797(2006).
CC   -!- FUNCTION: Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose).
CC       It could also play a role in the metabolism of some rare sugars such as
CC       L-fructose. Catalyzes the transfer of the gamma-phosphate group from
CC       ATP to the 1-hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-
CC       phosphate. Uridine triphosphate (UTP), cytidine 5-triphosphate (CTP),
CC       guanosine 5-triphosphate (GTP), and thymidine triphosphate (TTP) also
CC       can act as phosphoryl donors. It can also phosphorylate L-fuculose and
CC       L-xylulose. {ECO:0000255|HAMAP-Rule:MF_01535,
CC       ECO:0000269|PubMed:14264882, ECO:0000269|PubMed:16674975,
CC       ECO:0000269|PubMed:5341476}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-rhamnulose + ATP = L-rhamnulose 1-phosphate + ADP + H(+);
CC         Xref=Rhea:RHEA:20117, ChEBI:CHEBI:15378, ChEBI:CHEBI:17897,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58313, ChEBI:CHEBI:456216; EC=2.7.1.5;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01535,
CC         ECO:0000269|PubMed:14264882, ECO:0000269|PubMed:16674975};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01535, ECO:0000269|PubMed:14264882};
CC       Note=It can also use manganese, cobalt, iron, calcium and copper ions.
CC       {ECO:0000269|PubMed:14264882};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=82 uM for L-rhamnulose (at pH 8.5 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:14264882};
CC         KM=110 uM for ATP (at pH 8.5 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:14264882};
CC         KM=270 uM for magnesium ion (at pH 8.5 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:14264882};
CC         KM=3 mM for beta-L-fructose (at pH 8) {ECO:0000269|PubMed:16674975};
CC       pH dependence:
CC         Optimum pH is 8.5. {ECO:0000269|PubMed:14264882};
CC   -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation; glycerone
CC       phosphate from L-rhamnose: step 2/3. {ECO:0000255|HAMAP-Rule:MF_01535}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01535,
CC       ECO:0000269|PubMed:16674975}.
CC   -!- INDUCTION: Induced by L-rhamnose via the RhaR-RhaS regulatory cascade.
CC       Binding of the cAMP receptor protein (CRP) is required for full
CC       expression. Also induced by L-lyxose. {ECO:0000269|PubMed:10852886,
CC       ECO:0000269|PubMed:1650346, ECO:0000269|PubMed:8230210}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to utilize
CC       rhamnose as a source of carbon. {ECO:0000269|PubMed:5341476}.
CC   -!- SIMILARITY: Belongs to the rhamnulokinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01535}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA43001.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X60472; CAA43001.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; L19201; AAB03037.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76886.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77405.1; -; Genomic_DNA.
DR   PIR; S40848; S40848.
DR   RefSeq; NP_418340.1; NC_000913.3.
DR   RefSeq; WP_000144073.1; NZ_CP009789.1.
DR   PDB; 2CGJ; X-ray; 2.26 A; A=1-489.
DR   PDB; 2CGK; X-ray; 2.46 A; A/B=1-489.
DR   PDB; 2CGL; X-ray; 1.88 A; A=1-489.
DR   AlphaFoldDB; P32171; -.
DR   SMR; P32171; -.
DR   BioGRID; 4260677; 3.
DR   FunCoup; P32171; 379.
DR   IntAct; P32171; 2.
DR   STRING; 511145.b3904; -.
DR   PaxDb; 511145-b3904; -.
DR   EnsemblBacteria; AAC76886; AAC76886; b3904.
DR   GeneID; 948399; -.
DR   KEGG; ecj:JW3875; -.
DR   KEGG; eco:b3904; -.
DR   KEGG; ecoc:C3026_21105; -.
DR   PATRIC; fig|1411691.4.peg.2802; -.
DR   EchoBASE; EB1814; -.
DR   eggNOG; COG1070; Bacteria.
DR   HOGENOM; CLU_039395_0_0_6; -.
DR   InParanoid; P32171; -.
DR   OMA; HYRDART; -.
DR   OrthoDB; 9761504at2; -.
DR   PhylomeDB; P32171; -.
DR   BioCyc; EcoCyc:RHAMNULOKIN-MONOMER; -.
DR   BioCyc; MetaCyc:RHAMNULOKIN-MONOMER; -.
DR   BRENDA; 2.7.1.5; 2026.
DR   UniPathway; UPA00541; UER00602.
DR   EvolutionaryTrace; P32171; -.
DR   PRO; PR:P32171; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P32171; -.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0008993; F:rhamnulokinase activity; IDA:UniProtKB.
DR   GO; GO:0019301; P:rhamnose catabolic process; IDA:UniProtKB.
DR   CDD; cd07771; ASKHA_NBD_FGGY_RhaB-like; 1.
DR   FunFam; 3.30.420.40:FF:000064; Rhamnulokinase; 1.
DR   FunFam; 3.30.420.40:FF:000073; Rhamnulokinase; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_01535; Rhamnulokinase; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018485; FGGY_C.
DR   InterPro; IPR018484; FGGY_N.
DR   InterPro; IPR013449; Rhamnulokinase.
DR   NCBIfam; NF007925; PRK10640.1; 1.
DR   NCBIfam; TIGR02627; rhamnulo_kin; 1.
DR   PANTHER; PTHR10196:SF93; L-RHAMNULOKINASE; 1.
DR   PANTHER; PTHR10196; SUGAR KINASE; 1.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PDBsum; 2CGJ; -.
DR   PDBsum; 2CGK; -.
DR   PDBsum; 2CGL; -.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Disulfide bond; Kinase; Magnesium;
KW   Nucleotide-binding; Reference proteome; Rhamnose metabolism; Transferase.
FT   CHAIN           1..489
FT                   /note="L-Rhamnulokinase"
FT                   /id="PRO_0000090531"
FT   ACT_SITE        237
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535,
FT                   ECO:0000269|PubMed:16674975"
FT   BINDING         13..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535,
FT                   ECO:0000269|PubMed:16674975"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535,
FT                   ECO:0000269|PubMed:16674975"
FT   BINDING         236..238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535,
FT                   ECO:0000269|PubMed:16674975"
FT   BINDING         259
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535,
FT                   ECO:0000269|PubMed:16674975"
FT   BINDING         296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535,
FT                   ECO:0000269|PubMed:16674975"
FT   BINDING         304
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535,
FT                   ECO:0000269|PubMed:16674975"
FT   BINDING         402
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535,
FT                   ECO:0000269|PubMed:16674975"
FT   DISULFID        68..222
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535,
FT                   ECO:0000269|PubMed:16674975"
FT   DISULFID        353..370
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535,
FT                   ECO:0000269|PubMed:16674975"
FT   DISULFID        413..417
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT   MUTAGEN         69
FT                   /note="E->A: Same kinase activity as the wild-type; when
FT                   associated with A-70 and A-73."
FT                   /evidence="ECO:0000269|PubMed:16674975"
FT   MUTAGEN         70
FT                   /note="E->A: Same kinase activity as the wild-type; when
FT                   associated with A-69 and A-73."
FT                   /evidence="ECO:0000269|PubMed:16674975"
FT   MUTAGEN         73
FT                   /note="R->A: Same kinase activity as the wild-type; when
FT                   associated with A-69 and A-70."
FT                   /evidence="ECO:0000269|PubMed:16674975"
FT   CONFLICT        214
FT                   /note="Missing (in Ref. 1; CAA43001)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        388..389
FT                   /note="QL -> HV (in Ref. 1; CAA43001)"
FT                   /evidence="ECO:0000305"
FT   STRAND          4..11
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   STRAND          13..24
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           25..27
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   STRAND          29..39
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   STRAND          43..45
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   STRAND          48..50
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           53..69
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   STRAND          74..81
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   STRAND          86..89
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   STRAND          91..93
FT                   /evidence="ECO:0007829|PDB:2CGJ"
FT   STRAND          95..97
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           105..107
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           110..114
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           115..119
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           120..127
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           136..146
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           148..153
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   STRAND          156..159
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           160..169
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           176..179
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           180..182
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   TURN            187..189
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   STRAND          190..192
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           194..200
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           204..206
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           208..210
FT                   /evidence="ECO:0007829|PDB:2CGJ"
FT   STRAND          216..221
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   STRAND          223..225
FT                   /evidence="ECO:0007829|PDB:2CGK"
FT   STRAND          227..231
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           237..244
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   STRAND          252..269
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           274..279
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   STRAND          282..284
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           287..289
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   STRAND          291..297
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           301..309
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           315..322
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   STRAND          327..330
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           337..339
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           345..355
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           358..361
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           364..390
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   STRAND          395..401
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           402..405
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           407..417
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   STRAND          419..423
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           428..440
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           447..455
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   STRAND          461..463
FT                   /evidence="ECO:0007829|PDB:2CGL"
FT   HELIX           470..479
FT                   /evidence="ECO:0007829|PDB:2CGL"
SQ   SEQUENCE   489 AA;  54069 MW;  AF66259EACAC5F4E CRC64;
     MTFRNCVAVD LGASSGRVML ARYERECRSL TLREIHRFNN GLHSQNGYVT WDVDSLESAI
     RLGLNKVCEE GIRIDSIGID TWGVDFVLLD QQGQRVGLPV AYRDSRTNGL MAQAQQQLGK
     RDIYQRSGIQ FLPFNTLYQL RALTEQQPEL IPHIAHALLM PDYFSYRLTG KMNWEYTNAT
     TTQLVNINSD DWDESLLAWS GANKAWFGRP THPGNVIGHW ICPQGNEIPV VAVASHDTAS
     AVIASPLNGS RAAYLSSGTW SLMGFESQTP FTNDTALAAN ITNEGGAEGR YRVLKNIMGL
     WLLQRVLQEQ QINDLPALIS ATQALPACRF IINPNDDRFI NPETMCSEIQ AACRETAQPI
     PESDAELARC IFDSLALLYA DVLHELAQLR GEDFSQLHIV GGGCQNTLLN QLCADACGIR
     VIAGPVEAST LGNIGIQLMT LDELNNVDDF RQVVSTTANL TTFTPNPDSE IAHYVAQIHS
     TRQTKELCA
//