ID   Q31UM3_SHIBS            Unreviewed;       309 AA.
AC   Q31UM3;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Ribokinase {ECO:0000256|ARBA:ARBA00016943, ECO:0000256|HAMAP-Rule:MF_01987};
DE            Short=RK {ECO:0000256|HAMAP-Rule:MF_01987};
DE            EC=2.7.1.15 {ECO:0000256|ARBA:ARBA00012035, ECO:0000256|HAMAP-Rule:MF_01987};
GN   Name=rbsK {ECO:0000256|HAMAP-Rule:MF_01987,
GN   ECO:0000313|EMBL:ABB68235.1};
GN   OrderedLocusNames=SBO_3766 {ECO:0000313|EMBL:ABB68235.1};
OS   Shigella boydii serotype 4 (strain Sb227).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300268 {ECO:0000313|EMBL:ABB68235.1, ECO:0000313|Proteomes:UP000007067};
RN   [1] {ECO:0000313|EMBL:ABB68235.1, ECO:0000313|Proteomes:UP000007067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sb227 {ECO:0000313|EMBL:ABB68235.1,
RC   ECO:0000313|Proteomes:UP000007067};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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|ARBA:ARBA00000691,
CC         ECO:0000256|HAMAP-Rule:MF_01987};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         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}.
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DR   EMBL; CP000036; ABB68235.1; -; Genomic_DNA.
DR   RefSeq; WP_001300603.1; NC_007613.1.
DR   AlphaFoldDB; Q31UM3; -.
DR   SMR; Q31UM3; -.
DR   GeneID; 75205470; -.
DR   KEGG; sbo:SBO_3766; -.
DR   HOGENOM; CLU_027634_2_0_6; -.
DR   UniPathway; UPA00916; UER00889.
DR   Proteomes; UP000007067; 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   NCBIfam; TIGR02152; D_ribokin_bact; 1.
DR   PANTHER; PTHR10584:SF166; RIBOKINASE; 1.
DR   PANTHER; PTHR10584; SUGAR KINASE; 1.
DR   Pfam; PF00294; PfkB; 1.
DR   PRINTS; PR00990; RIBOKINASE.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
DR   PROSITE; PS00584; PFKB_KINASES_2; 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:0000256|RuleBase:RU003704};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01987};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01987}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_01987};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01987}.
FT   DOMAIN          6..297
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
FT   ACT_SITE        255
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         14..16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         42..46
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         223..228
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         249
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         251
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         254..255
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         279
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         285
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         288
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         290
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         294
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
SQ   SEQUENCE   309 AA;  32291 MW;  753729B41E64060E CRC64;
     MQNAGSLVVL GSINADHILN LQSFPTPGET VTGNHYQVAF GGKGANQAVA AGRSGANIAF
     IACTGDDSIG ESVRQQLATD NIDITPVSVI KGESTGVALI FVNGEGENVI GIHAGANAAL
     SPALVEAQRE RIANASALLM QLESPLESVM AAAKIAHQNK TIVALNPAPA RELPDELLAL
     VDIITPNETE AEKLTGIRVE NDEDAAKAAQ VLHEKGIRTV LITLGSRGVW ASVNGEGQRV
     PGFRVQAVDT IAAGDTFNGA LITALLEEKP LPEAIRFAHA AAAIAVTRKG AQPSVPWREE
     IDAFLDRQR
//