ID D3H533_ECO44 Unreviewed; 489 AA.
AC D3H533;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Rhamnulokinase {ECO:0000256|HAMAP-Rule:MF_01535};
DE Short=RhaB {ECO:0000256|HAMAP-Rule:MF_01535};
DE EC=2.7.1.5 {ECO:0000256|HAMAP-Rule:MF_01535};
DE AltName: Full=ATP:L-rhamnulose phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01535};
DE AltName: Full=L-rhamnulose 1-kinase {ECO:0000256|HAMAP-Rule:MF_01535};
DE AltName: Full=Rhamnulose kinase {ECO:0000256|HAMAP-Rule:MF_01535};
GN Name=rhaB {ECO:0000256|HAMAP-Rule:MF_01535,
GN ECO:0000313|EMBL:CBG37102.1};
GN OrderedLocusNames=EC042_4277 {ECO:0000313|EMBL:CBG37102.1};
OS Escherichia coli O44:H18 (strain 042 / EAEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=216592 {ECO:0000313|EMBL:CBG37102.1, ECO:0000313|Proteomes:UP000001407};
RN [1] {ECO:0000313|EMBL:CBG37102.1, ECO:0000313|Proteomes:UP000001407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=042 / EAEC {ECO:0000313|Proteomes:UP000001407};
RX PubMed=20098708; DOI=10.1371/journal.pone.0008801;
RA Chaudhuri R.R., Sebaihia M., Hobman J.L., Webber M.A., Leyton D.L.,
RA Goldberg M.D., Cunningham A.F., Scott-Tucker A., Ferguson P.R.,
RA Thomas C.M., Frankel G., Tang C.M., Dudley E.G., Roberts I.S., Rasko D.A.,
RA Pallen M.J., Parkhill J., Nataro J.P., Thomson N.R., Henderson I.R.;
RT "Complete genome sequence and comparative metabolic profiling of the
RT prototypical enteroaggregative Escherichia coli strain 042.";
RL PLoS ONE 5:E8801-E8801(2010).
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:0000256|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:0000256|HAMAP-Rule:MF_01535};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01535};
CC -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation; glycerone
CC phosphate from L-rhamnose: step 2/3. {ECO:0000256|HAMAP-Rule:MF_01535}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01535}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family.
CC {ECO:0000256|ARBA:ARBA00009156}.
CC -!- SIMILARITY: Belongs to the rhamnulokinase family. {ECO:0000256|HAMAP-
CC Rule:MF_01535}.
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DR EMBL; FN554766; CBG37102.1; -; Genomic_DNA.
DR RefSeq; WP_000144086.1; NC_017626.1.
DR AlphaFoldDB; D3H533; -.
DR KEGG; elo:EC042_4277; -.
DR PATRIC; fig|216592.3.peg.4437; -.
DR HOGENOM; CLU_039395_0_0_6; -.
DR UniPathway; UPA00541; UER00602.
DR Proteomes; UP000001407; 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 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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01535};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW Rule:MF_01535}; Kinase {ECO:0000256|HAMAP-Rule:MF_01535};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01535};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01535};
KW Rhamnose metabolism {ECO:0000256|ARBA:ARBA00023308, ECO:0000256|HAMAP-
KW Rule:MF_01535};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01535}.
FT DOMAIN 7..242
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 253..440
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT ACT_SITE 237
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 13..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 236..238
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 259
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT DISULFID 68..222
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT DISULFID 353..370
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT DISULFID 413..417
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
SQ SEQUENCE 489 AA; 54060 MW; B44D62D9B918D07D CRC64;
MTFRNCVAVD LGASSGRVML ARYERECRSL TLREIHRFNN GLHSQNGYVT WDVDSLESAI
RLGLNKVCEE GIRIDSIGID TWGVDFVLLD QQGQRVGLPV AYRDSRTNGL MAQAQQQLGK
RNIYQRSGIQ FLPFNTLYQL HALTEQQPEL IPHIAHALLM PDYFSYRLTG KMNWEYTNAT
TTQLVNINSD DWDESLLAWS GANKAWFGRP THPGNVIGHW ICPQSNEIPV VAVASHDTAS
AVIASPLNGS RAAYLSSGTW SLMGFESQTP FTNDTALAAN ITNEGGAEGR YRVLKNIMGL
WLLQRVLQER QINDLPALIA ATQGLQACRF IINPNDDRFI NPEAMCSEIQ AACRETAQPI
PESDAELARC IFDSLALLYA DVLHELAQLR GEDFSQLHIV GGGCQNALLN QLCADACGIR
VIAGPVEAST LGNIGIQLMT LDELNNVDDF RQVVSTTANL TTFIPNPDSE IAHYVAQIHS
TRQTKELCA
//
