RHAB_LISMO
ID RHAB_LISMO Reviewed; 483 AA.
AC Q8Y3I6;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=lmo2849;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; AL591984; CAD01062.1; -; Genomic_DNA.
DR PIR; AH1430; AH1430.
DR RefSeq; NP_466371.1; NC_003210.1.
DR RefSeq; WP_009924505.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y3I6; -.
DR SMR; Q8Y3I6; -.
DR STRING; 169963.lmo2849; -.
DR PaxDb; Q8Y3I6; -.
DR EnsemblBacteria; CAD01062; CAD01062; CAD01062.
DR GeneID; 986385; -.
DR KEGG; lmo:lmo2849; -.
DR PATRIC; fig|169963.11.peg.2920; -.
DR eggNOG; COG1070; Bacteria.
DR HOGENOM; CLU_039395_0_1_9; -.
DR OMA; GNLLMQM; -.
DR PhylomeDB; Q8Y3I6; -.
DR BioCyc; LMON169963:LMO2849-MON; -.
DR UniPathway; UPA00541; UER00602.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
DR GO; GO:0008993; F:rhamnulokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019301; P:rhamnose catabolic process; IBA:GO_Central.
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; Nucleotide-binding;
KW Reference proteome; Rhamnose metabolism; Transferase.
FT CHAIN 1..483
FT /note="Rhamnulokinase"
FT /id="PRO_0000090539"
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"
FT DISULFID 352..369
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
SQ SEQUENCE 483 AA; 54757 MW; 2B5F2D541BCEE4FD CRC64;
MKHYVAVDIG ASSGRLILGK LVNEKLQLEE IHRFKNGFTY RDGHERWEID QLMQEIFIGL
EKVKQLGISE CVLGIDTWGV DYVLIGASGE KLADPISYRD KRTLNAVQNL TSEYPREYIY
KKTGIQFMEL NTLYQLYVEE RDLLERAEKI LLIPDYIGYV LTGVKVAETT NSSTTQMLNL
REQLFDKDLL SHLNIDVEKF APLTDAGTYL GEVKEDWLKM YDIPNCDVVT VATHDTASAV
VGTPAEGENW AFLSSGTWSL IGMELSAPIN NEVAFKENYT NEWGAYGTYR FLKNIMGLWI
VQEIARMDDY KHSFAEMAEE AGNYPYFKQI INVNDARFNN PENMVDEIRL YCRETGQTVP
ETIGELTNCV YGSLALYYAL ELEKMTEITG KKIEKLYIVG GGSNVAMLNQ LTAKLAGIEV
FAGPSEATAI GNLVVQMINQ GEIESMRAGR KIIRNSFEIG EFSCGDVRFE EIKERFTKVL
EFN
