ID   RHAB_ECO24              Reviewed;         489 AA.
AC   A7ZUB5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Rhamnulokinase {ECO:0000255|HAMAP-Rule:MF_01535};
DE            Short=RhaB {ECO:0000255|HAMAP-Rule:MF_01535};
DE            EC=2.7.1.5 {ECO:0000255|HAMAP-Rule:MF_01535};
DE   AltName: Full=ATP:L-rhamnulose phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01535};
DE   AltName: Full=L-rhamnulose 1-kinase {ECO:0000255|HAMAP-Rule:MF_01535};
DE   AltName: Full=Rhamnulose kinase {ECO:0000255|HAMAP-Rule:MF_01535};
GN   Name=rhaB {ECO:0000255|HAMAP-Rule:MF_01535};
GN   OrderedLocusNames=EcE24377A_4435;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
CC   -!- FUNCTION: Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose).
CC       Catalyzes the transfer of the gamma-phosphate group from ATP to the 1-
CC       hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_01535}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01535};
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   -!- SIMILARITY: Belongs to the rhamnulokinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01535}.
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DR   EMBL; CP000800; ABV17166.1; -; Genomic_DNA.
DR   RefSeq; WP_000144052.1; NC_009801.1.
DR   AlphaFoldDB; A7ZUB5; -.
DR   SMR; A7ZUB5; -.
DR   EnsemblBacteria; ABV17166; ABV17166; EcE24377A_4435.
DR   KEGG; ecw:EcE24377A_4435; -.
DR   HOGENOM; CLU_039395_0_0_6; -.
DR   OMA; MPDLFNY; -.
DR   UniPathway; UPA00541; UER00602.
DR   Proteomes; UP000001122; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008993; F:rhamnulokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019301; P:rhamnose catabolic process; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   ATP-binding; Disulfide bond; Kinase; Magnesium; Nucleotide-binding;
KW   Rhamnose metabolism; Transferase.
FT   CHAIN           1..489
FT                   /note="Rhamnulokinase"
FT                   /id="PRO_1000068715"
FT   ACT_SITE        237
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT   BINDING         13..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT   BINDING         236..238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT   BINDING         259
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT   BINDING         296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT   BINDING         304
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT   BINDING         402
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT   DISULFID        68..222
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT   DISULFID        353..370
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT   DISULFID        413..417
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
SQ   SEQUENCE   489 AA;  54050 MW;  45D5661851B7DAFD CRC64;
     MTFRNCVAVD LGASSGRVML ARYERECRSL TLREIHRFKN GLHSQNGYVT WNVDSLESAI
     RLGLNKVCEE GIRIDSIGID TWGVDFVLLD QQGQRVGLPV AYRDSRSNGL MAQAQQQLGK
     RDIYQRSGIQ FLPFNTLYQL RALTEQQPEL IPHIAHALLM PDYFSYRLTG KMNWEYTNAT
     TTQLVNINSD DWDESLLAWS GANKAWFGRP THPGNVIGHW ICPQGNEIPV VAVASHDTAS
     AVIASPLNGS RAAYLSSGTW SLMGFESQTP FTNDTALAAN ITNEGGAEGR YRVLKNIMGL
     WLLQRVLQER QINDLPALIA ATQALPACRF IINPNDDRFI NPEAMCSEIQ AACRETAQPI
     PESDAELARC IFDSLALLYA DVLHELAQLR GEDFSQLHIV GGGCQNTLLN QLCADACGIR
     VIAGPVEAST LGNIGIQLMT LDELNNVDDF RQVVSTTANL TTFTPNPDSE IAHYVAQIHS
     TRQTKELCA