RHAB_ECOLI
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 03-AUG-2022, entry version 148.
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, ECO:0000303|PubMed:8396120};
GN OrderedLocusNames=b3904, JW3875;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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=ATP + L-rhamnulose = ADP + H(+) + L-rhamnulose 1-phosphate;
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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01535,
CC 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_SSZK01000014.1.
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 PDBsum; 2CGJ; -.
DR PDBsum; 2CGK; -.
DR PDBsum; 2CGL; -.
DR AlphaFoldDB; P32171; -.
DR SMR; P32171; -.
DR IntAct; P32171; 2.
DR STRING; 511145.b3904; -.
DR PaxDb; P32171; -.
DR PRIDE; P32171; -.
DR EnsemblBacteria; AAC76886; AAC76886; b3904.
DR EnsemblBacteria; BAE77405; BAE77405; BAE77405.
DR GeneID; 948399; -.
DR KEGG; ecj:JW3875; -.
DR KEGG; eco:b3904; -.
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; MPDLFNY; -.
DR PhylomeDB; P32171; -.
DR BioCyc; EcoCyc:RHAMNULOKIN-MON; -.
DR BioCyc; MetaCyc:RHAMNULOKIN-MON; -.
DR BRENDA; 2.7.1.5; 2026.
DR UniPathway; UPA00541; UER00602.
DR EvolutionaryTrace; P32171; -.
DR PRO; PR:P32171; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
DR GO; GO:0008993; F:rhamnulokinase activity; IDA:UniProtKB.
DR GO; GO:0019301; P:rhamnose catabolic process; IDA:UniProtKB.
DR CDD; cd07771; FGGY_RhuK; 1.
DR HAMAP; MF_01535; Rhamnulokinase; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR013449; Rhamnulokinase.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR02627; rhamnulo_kin; 1.
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 TURN 25..28
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..118
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 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 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
