RHAB_LACPL
ID RHAB_LACPL Reviewed; 488 AA.
AC Q88S49; F9ULE9;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=lp_3595;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
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; AL935263; CCC80556.1; -; Genomic_DNA.
DR RefSeq; WP_003642942.1; NC_004567.2.
DR RefSeq; YP_004891070.1; NC_004567.2.
DR AlphaFoldDB; Q88S49; -.
DR SMR; Q88S49; -.
DR STRING; 220668.lp_3595; -.
DR EnsemblBacteria; CCC80556; CCC80556; lp_3595.
DR GeneID; 57026789; -.
DR KEGG; lpl:lp_3595; -.
DR PATRIC; fig|220668.9.peg.3000; -.
DR eggNOG; COG1070; Bacteria.
DR HOGENOM; CLU_039395_0_1_9; -.
DR OMA; GNLLMQM; -.
DR PhylomeDB; Q88S49; -.
DR BioCyc; LPLA220668:G1GW0-3043-MON; -.
DR UniPathway; UPA00541; UER00602.
DR Proteomes; UP000000432; 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; Kinase; Magnesium; Nucleotide-binding; Reference proteome;
KW Rhamnose metabolism; Transferase.
FT CHAIN 1..488
FT /note="Rhamnulokinase"
FT /id="PRO_0000090536"
FT ACT_SITE 235
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 11..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 234..236
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 401
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
SQ SEQUENCE 488 AA; 55266 MW; 1155DC33710FD9FA CRC64;
MKSYIAVDIG ASSGRLMLGQ QKRGQLTLKE VHRFSNGFAM KDGHDRWDVD HLIHEIFKGL
EKVKKMGIKD VELGIDTWAV DYVLVGENGH KLEDPISYRD KRTHNAIQQL TSDLPKEYIY
EKTGIQFQDF NTLYQLYKEN HDLLAKTDKI MMMPDYLGYV LTGNAVTEIT NASTTQMLNL
RVGLFDKDLL GKVNVSQDQF PRLVESGSVL GNVSHKWHTQ YDIPEVEVVT VATHDTASAV
VGTPGEGDRW AFLSSGTWSL LGTELNVPEN GLQAFHENYT NEWGAYGTYR FLKNIMGLWV
AQCVRHELGD QYSFGELADL AQQVRPFQQF IDINDERFTN PENMIKELQD YCRETKQTIP
ETPGELFQAI YSNLSLFYAN ELNKLDRILG YHIDTLNIVG GGSNVALMNQ LTSTLANIKV
VAGPSEATAV GNIMVQMITS DEVENIGAGR RLIETSFDLK RYLPETNKYG DILKEYQRFL
TNKSKEMV
