ID   C7MI29_BRAFD            Unreviewed;       309 AA.
AC   C7MI29;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   17-JUN-2020, entry version 58.
DE   RecName: Full=Ribokinase {ECO:0000256|HAMAP-Rule:MF_01987};
DE            Short=RK {ECO:0000256|HAMAP-Rule:MF_01987};
DE            EC=2.7.1.15 {ECO:0000256|HAMAP-Rule:MF_01987};
GN   Name=rbsK {ECO:0000256|HAMAP-Rule:MF_01987};
GN   OrderedLocusNames=Bfae_05890 {ECO:0000313|EMBL:ACU84455.1};
OS   Brachybacterium faecium (strain ATCC 43885 / DSM 4810 / NCIB 9860).
OC   Bacteria; Actinobacteria; Micrococcales; Dermabacteraceae; Brachybacterium.
OX   NCBI_TaxID=446465 {ECO:0000313|EMBL:ACU84455.1, ECO:0000313|Proteomes:UP000001919};
RN   [1] {ECO:0000313|EMBL:ACU84455.1, ECO:0000313|Proteomes:UP000001919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43885 / DSM 4810 / NCIB 9860
RC   {ECO:0000313|Proteomes:UP000001919};
RX   PubMed=21304631; DOI=10.4056/sigs.492;
RA   Lapidus A., Pukall R., Labuttii K., Copeland A., Del Rio T.G., Nolan M.,
RA   Chen F., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Rohde M., Goker M., Pati A., Ivanova N., Mavrommatis K., Chen A.,
RA   Palaniappan K., D'haeseleer P., Chain P., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Brachybacterium faecium type strain
RT   (Schefferle 6-10).";
RL   Stand. Genomic Sci. 1:3-11(2009).
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:0000256|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:0000256|HAMAP-Rule:MF_01987};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01987}.
CC   -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-
CC       phosphate from beta-D-ribopyranose: step 2/2. {ECO:0000256|HAMAP-
CC       Rule:MF_01987}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01987}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987}.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. Ribokinase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01987}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01987}.
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DR   EMBL; CP001643; ACU84455.1; -; Genomic_DNA.
DR   RefSeq; WP_012804230.1; NC_013172.1.
DR   RefSeq; YP_003154045.1; NC_013172.1.
DR   STRING; 446465.Bfae_05890; -.
DR   EnsemblBacteria; ACU84455; ACU84455; Bfae_05890.
DR   GeneID; 8399137; -.
DR   KEGG; bfa:Bfae_05890; -.
DR   PATRIC; fig|446465.5.peg.577; -.
DR   eggNOG; ENOG4108RVA; Bacteria.
DR   eggNOG; COG0524; LUCA.
DR   HOGENOM; CLU_027634_2_0_11; -.
DR   KO; K00852; -.
DR   OMA; CDYITPN; -.
DR   OrthoDB; 1030724at2; -.
DR   BioCyc; BFAE446465:G1GF4-586-MONOMER; -.
DR   UniPathway; UPA00916; UER00889.
DR   Proteomes; UP000001919; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01987, ECO:0000313|EMBL:ACU84455.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001919};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   DOMAIN          8..295
FT                   /note="PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
FT   NP_BIND         252..253
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   REGION          15..17
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   REGION          43..47
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   REGION          287..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        253
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   METAL           247
FT                   /note="Potassium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   METAL           249
FT                   /note="Potassium; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   METAL           283
FT                   /note="Potassium; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   METAL           286
FT                   /note="Potassium; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   METAL           288
FT                   /note="Potassium; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   METAL           292
FT                   /note="Potassium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         141
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         185
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         253
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
SQ   SEQUENCE   309 AA;  31515 MW;  43D706D0F15A2E8D CRC64;
     MPARPAPVLV VGSATVDVTS FSQRLPQPGE TLLGDSFSLV MGGKGANQAV AAARAGAQAR
     FVGCVGEDMF APVVRDGLGE AGVDLTHLRT VPGQTGVAHI RVDGAGENDI VMVPLANSAL
     STAQIDEALD DDAGVLLTQL ETPLPETLHA IRAAHEQGLT VVLDPAPAAE LDPAIWPLLD
     VVTPNETEAA LLTGMPVRDR EGAVRAGRWF LARGTRAALI TLAGAGSVLV TAQEVHEIPP
     HPVTVVDSTA AGDAFAGFLA AALADGEDLP SAVRRAGAAG ALAVTRRGAS PSIPSADEAQ
     RMLDEEVPA
//