ID   RHAB_ECOK1              Reviewed;         489 AA.
AC   A1AI81;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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}; OrderedLocusNames=Ecok1_38770;
GN   ORFNames=APECO1_2564;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABJ03371.1; -; Genomic_DNA.
DR   RefSeq; WP_000144110.1; NC_008563.1.
DR   AlphaFoldDB; A1AI81; -.
DR   SMR; A1AI81; -.
DR   EnsemblBacteria; ABJ03371; ABJ03371; APECO1_2564.
DR   KEGG; ecv:APECO1_2564; -.
DR   HOGENOM; CLU_039395_0_0_6; -.
DR   OMA; MPDLFNY; -.
DR   UniPathway; UPA00541; UER00602.
DR   Proteomes; UP000008216; 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_0000297520"
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;  54076 MW;  E2B573E7AE58CA24 CRC64;
     MTFRNCVAVD LGASSGRVML ARYERECRSL TLREIHRFNN GLHSQNGYVT WNVDSLESAI
     RLGLNKVCEE GIRIDSIGID TWGVDFVLLD QQGQRVGLPV AYRDSRTNGL MAQAQQQLGK
     RDIYQRSGIQ FLPFNTIYQL RALTEQQPEL IPHIAHALLI PDYFSYRLTG KMNWEYTNAT
     TTQLVNINSD DWDESLLAWS GANKAWFGRP THPGNVIGHW ICPQGNEIPV VAVASHDTAS
     AVIASPLNGS RAAYLSSGTW SLMGFESQTP FTNDTALAAN ITNEGGAEGR YRVLKNIMGL
     WLLQRVLQER QINDLPALIA ATQALPACRF IINPNDDRFI NPDEMCSEIQ AACRETAQPI
     PESDAELARC IFDSLALLYA DVLHELAQLR GEDFSQLHIV GGGCQNTLLN QLCADACGIR
     VIAGPVEAST LGNIGIQLMT LDELNNVDDF RQVVSTTANL TTFTPNPDSE IAHYVAQIHS
     TRQTKELCA