RHAB_YERPS
ID RHAB_YERPS Reviewed; 485 AA.
AC Q66FF3;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=YPTB0385;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH19625.1; -; Genomic_DNA.
DR RefSeq; WP_002209105.1; NZ_CP009712.1.
DR AlphaFoldDB; Q66FF3; -.
DR SMR; Q66FF3; -.
DR EnsemblBacteria; CAH19625; CAH19625; YPTB0385.
DR GeneID; 66843200; -.
DR KEGG; yps:YPTB0385; -.
DR OMA; MPDLFNY; -.
DR UniPathway; UPA00541; UER00602.
DR Proteomes; UP000001011; 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 Rhamnose metabolism; Transferase.
FT CHAIN 1..485
FT /note="Rhamnulokinase"
FT /id="PRO_0000090548"
FT ACT_SITE 232
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 8..12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 231..233
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 397
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT DISULFID 348..365
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT DISULFID 408..412
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
SQ SEQUENCE 485 AA; 53424 MW; 813B36936B49AEA5 CRC64;
MVAIDLGASS GRVMLASYYP GQQQLTLREV CRFTNQIKSI DGSDVWDIDA IEQSIREGLS
QLDSEGIALD SIGIDSWGVD FVLLDKQGKR IGQPVSYRDS RTQGVMARAQ QTLGSNAIYR
RTGIQFLPFN TLYQLRALSE QQPHLLADVA HLLLIPDYLH YRLTGQLNWE YTNASTTQLL
NIETGDWDSD LLAYAGVPAH WFAKPGKPGN TIGYWHSANG QQVPVVAVAT HDTASAVLAA
PLIDADAAYL SSGTWSLMGF ESGTPLTHQQ AQCSNITNEG GAEGRYRVLK NIMGLWLLQR
ATDELQIDDL PQLIEQAARQ PACRSLINPN DSRFINPPNM CREIQNACRE HQFPVPNTAA
QLARCIFDSL AMLYRQVAQE LATLRGRPIS HLHIVGGGCQ NQFLNQLCAD ACGLNVSMGP
VEASTLGNIG SQLISLGEVA DVTHYRRIVA NNFPLHHLSP HDNSDFAAHW LQFQSLSQLP
KELCI
