RHAB_ENTFA
ID RHAB_ENTFA Reviewed; 494 AA.
AC Q838L3;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=EF_0433;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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 -!- SIMILARITY: Belongs to the rhamnulokinase family. {ECO:0000255|HAMAP-
CC Rule:MF_01535}.
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DR EMBL; AE016830; AAO80289.1; -; Genomic_DNA.
DR RefSeq; NP_814218.1; NC_004668.1.
DR RefSeq; WP_010706744.1; NZ_KE136524.1.
DR AlphaFoldDB; Q838L3; -.
DR SMR; Q838L3; -.
DR STRING; 226185.EF_0433; -.
DR EnsemblBacteria; AAO80289; AAO80289; EF_0433.
DR KEGG; efa:EF0433; -.
DR PATRIC; fig|226185.45.peg.2900; -.
DR eggNOG; COG1070; Bacteria.
DR HOGENOM; CLU_039395_0_1_9; -.
DR OMA; GNLLMQM; -.
DR UniPathway; UPA00541; UER00602.
DR Proteomes; UP000001415; 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; IPR000577; Carb_kinase_FGGY.
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 PIRSF; PIRSF000538; GlpK; 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 Reference proteome; Rhamnose metabolism; Transferase.
FT CHAIN 1..494
FT /note="Rhamnulokinase"
FT /id="PRO_0000090534"
FT ACT_SITE 243
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 18..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 242..244
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 310
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 411
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT DISULFID 360..377
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
SQ SEQUENCE 494 AA; 54916 MW; 8F0BFFBB37BB2C4B CRC64;
MKKEQVEKRT YLAVDIGASS GRIMKSQRLA NGQITIEEIH RFKNGFHQKD GYQRWDMASL
VHELLLGLQK VKQLGIKECF IGIDTWGVDY CLLDQSGQLL DEPIAYRDGR TEAAVTNFSK
GYSLEKLYQQ TGIQVQPFNT IFQLFVEEKE RLAAASQLLL IPDYLGYVFT GKAVIEATNA
STTQLLNAGT KQWESELLDF LGIDETLFPT LVEPGTILGD LQTAAFPDYD LPNATLITIA
SHDTASAILG TPGIGDDWAY ISSGTWSLLG IETTVTTISA EAFQENYTNE WGAQNTIRFL
KNIMGMWLIQ EVARHQNYQY SYAELAALAE KEPAFQQFID VNDPRFLNPG NMITELQAYC
RETQQTVPES PGELARCIYD NLALCYSVEL EKLAQLTGIE RKITTLHVVG GGSNNRLLNQ
LTADVANVTV NAGPGEAIAL GNLLMQMIAT GELKDIPAAR TCIQTSFPTE IYQANPIDST
IKNRYQAFMK RSSL
