ID   RHAB_ALKHC              Reviewed;         467 AA.
AC   Q9KCM0;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=BH1551;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB05270.1; -; Genomic_DNA.
DR   PIR; G83843; G83843.
DR   RefSeq; WP_010897714.1; NC_002570.2.
DR   AlphaFoldDB; Q9KCM0; -.
DR   SMR; Q9KCM0; -.
DR   STRING; 272558.10174168; -.
DR   EnsemblBacteria; BAB05270; BAB05270; BAB05270.
DR   KEGG; bha:BH1551; -.
DR   eggNOG; COG1070; Bacteria.
DR   HOGENOM; CLU_039395_0_1_9; -.
DR   OMA; GNLLMQM; -.
DR   OrthoDB; 1619686at2; -.
DR   UniPathway; UPA00541; UER00602.
DR   Proteomes; UP000001258; 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..467
FT                   /note="Rhamnulokinase"
FT                   /id="PRO_0000090528"
FT   ACT_SITE        236
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         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT   BINDING         235..237
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         400
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT   DISULFID        351..368
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
SQ   SEQUENCE   467 AA;  53111 MW;  A1EE48B71F088D8A CRC64;
     MNYSLAVDIG ASSGRLIVGE CNKKIQLTEI HRFENQIIEK NGQFCWDVDA LFSEIKTGLK
     KCREAGIEPV SMGIDTWAVD FVLLDEHDKP LTDAVSYRDP RTDGVMEEVI EQFMKERLYL
     ETGIQFQQFN TIYQLYALKK QHPDIFKKAK SFLMIPDYFH FLLTGKKANE YTNATTTQLV
     NAFTKKWDKD IIEALGFNPD MFQEIKLPTE SLGKLKSEWV EEVGFDLEVI LPATHDTGSA
     VVAVPKVADT IYLSSGTWSL IGVENSFPIC VTKALDYNFT NEGGMNYQFR FLKNIMGLWM
     IQEVRRNYDN RYSFAQLVEL SKGISFKSTV DVNDPRFLKP TNMIKEIQRY CQETGQQAPE
     LPGEVAKCVF ESLAESYTSA VAEIEDIFEK DFKSINVIGG GCRNELLNQL IADRTKKDVF
     AGPIEATAIG NLVAQWMALG EIESIQQARK LIYDSFDVKR YVSADRE