RBSK_ALKHC
ID RBSK_ALKHC Reviewed; 294 AA.
AC Q9K6K1;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Ribokinase {ECO:0000255|HAMAP-Rule:MF_01987};
DE Short=RK {ECO:0000255|HAMAP-Rule:MF_01987};
DE EC=2.7.1.15 {ECO:0000255|HAMAP-Rule:MF_01987};
GN Name=rbsK {ECO:0000255|HAMAP-Rule:MF_01987}; OrderedLocusNames=BH3728;
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: Catalyzes the phosphorylation of ribose at O-5 in a reaction
CC requiring ATP and magnesium. The resulting D-ribose-5-phosphate can
CC then be used either for sythesis of nucleotides, histidine, and
CC tryptophan, or as a component of the pentose phosphate pathway.
CC {ECO:0000255|HAMAP-Rule:MF_01987}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+);
CC Xref=Rhea:RHEA:13697, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:47013, ChEBI:CHEBI:78346, ChEBI:CHEBI:456216;
CC EC=2.7.1.15; Evidence={ECO:0000255|HAMAP-Rule:MF_01987};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01987};
CC Note=Requires a divalent cation, most likely magnesium in vivo, as an
CC electrophilic catalyst to aid phosphoryl group transfer. It is the
CC chelate of the metal and the nucleotide that is the actual substrate.
CC {ECO:0000255|HAMAP-Rule:MF_01987};
CC -!- ACTIVITY REGULATION: Activated by a monovalent cation that binds near,
CC but not in, the active site. The most likely occupant of the site in
CC vivo is potassium. Ion binding induces a conformational change that may
CC alter substrate affinity. {ECO:0000255|HAMAP-Rule:MF_01987}.
CC -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-
CC phosphate from beta-D-ribopyranose: step 2/2. {ECO:0000255|HAMAP-
CC Rule:MF_01987}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01987}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01987}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. Ribokinase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01987}.
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DR EMBL; BA000004; BAB07447.1; -; Genomic_DNA.
DR PIR; H84115; H84115.
DR RefSeq; WP_010899853.1; NC_002570.2.
DR AlphaFoldDB; Q9K6K1; -.
DR SMR; Q9K6K1; -.
DR STRING; 272558.10176352; -.
DR EnsemblBacteria; BAB07447; BAB07447; BAB07447.
DR KEGG; bha:BH3728; -.
DR eggNOG; COG0524; Bacteria.
DR HOGENOM; CLU_027634_2_2_9; -.
DR OMA; IPWRDEL; -.
DR OrthoDB; 1030724at2; -.
DR UniPathway; UPA00916; UER00889.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004747; F:ribokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019303; P:D-ribose catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01174; ribokinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR HAMAP; MF_01987; Ribokinase; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011877; D_ribokin.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR002139; Ribo/fructo_kinase.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR PRINTS; PR00990; RIBOKINASE.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR02152; D_ribokin_bact; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Carbohydrate metabolism; Cytoplasm; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Potassium; Reference proteome;
KW Transferase.
FT CHAIN 1..294
FT /note="Ribokinase"
FT /id="PRO_0000080095"
FT ACT_SITE 240
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987"
FT BINDING 13..15
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987"
FT BINDING 41..45
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987"
FT BINDING 185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987"
FT BINDING 208..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987"
FT BINDING 234
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987"
FT BINDING 236
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987"
FT BINDING 239..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987"
FT BINDING 263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987"
FT BINDING 269
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987"
FT BINDING 272
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987"
FT BINDING 274
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987"
SQ SEQUENCE 294 AA; 31089 MW; 8C13E0FCF5E89FDE CRC64;
MKTPNITVVG SINMDMVTIT DVVPVQGETV LGKDFRTVPG GKGANQAVAA ARLGANVRMI
GRVGDDPFGH VLTENLAKEG IITDSVKPVT DCTSGVATIL LSDRDNRIIV TKGANEHVTP
DYVAAFEQEL AASDVVLLQL EIPLETVAYV LEFCAKHHVT TVLNPAPAQK LPDAAWTDAT
YISPNENECL QLFGDEPDAN LRQKLIMTKG ADGVQFYEND EQVQVESFRV EPVDTTGAGD
TFNGAFAVAL GGGTVKEAVR FANAAAALSV QSFGAQGGMP TKAQVQSFLQ EQGG
