ID   A0A078RU34_BACUN        Unreviewed;       298 AA.
AC   A0A078RU34;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 30.
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:KDS47989.1};
GN   ORFNames=M094_2921 {ECO:0000313|EMBL:KDS47989.1};
OS   Bacteroides uniformis str. 3978 T3 ii.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1339349 {ECO:0000313|EMBL:KDS47989.1, ECO:0000313|Proteomes:UP000028013};
RN   [1] {ECO:0000313|EMBL:KDS47989.1, ECO:0000313|Proteomes:UP000028013}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3978 T3 ii {ECO:0000313|EMBL:KDS47989.1,
RC   ECO:0000313|Proteomes:UP000028013};
RA   Sears C., Carroll K., Sack B.R., Qadri F., Myers L.L., Chung G.-T.,
RA   Escheverria P., Fraser C.M., Sadzewicz L., Shefchek K.A., Tallon L.,
RA   Das S.P., Daugherty S., Mongodin E.F.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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;
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   -!- SIMILARITY: Belongs to the carbohydrate kinase pfkB family.
CC       {ECO:0000256|ARBA:ARBA00005380}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01987}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDS47989.1}.
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DR   EMBL; JNHN01000184; KDS47989.1; -; Genomic_DNA.
DR   RefSeq; WP_035447294.1; NZ_JNHN01000184.1.
DR   EnsemblBacteria; KDS47989; KDS47989; M094_2921.
DR   PATRIC; fig|1339349.3.peg.3975; -.
DR   UniPathway; UPA00916; UER00889.
DR   Proteomes; UP000028013; Unassembled WGS sequence.
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; PS00583; PFKB_KINASES_1; 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|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01987};
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          1..293
FT                   /note="PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
FT   REGION          11..13
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   REGION          39..43
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   ACT_SITE        252
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         220..225
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         246
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         248
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         251..252
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         282
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
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         287
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT   BINDING         291
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
SQ   SEQUENCE   298 AA;  31927 MW;  A46DDDB99B87EC35 CRC64;
     MKKIIVIGSS NVDMVVRTSH LPAPGETILG GEFFMNQGGK GANQAVAIKR LGGNLIFMAK
     LGNDVLGRQS VGYFKKEGID TRYIALDEDS ASGVALISVD DHAENSIVVA SGANMLLNEQ
     DVDKMLEEMC EGDILLMQLE IPLQTVEYAA RKAFGKGVKV VLNPAPARSL PKELFRHLYM
     VTPNRIEAEM LTGIKIANDA DVEKVAEEIC AMGVKNVIIT LGSKGCLIRE EGVSYRIDAF
     KVEPVDTTAA GDTFNGALCV GLSEGMDLKQ AAVMASKASS IAVTRMGAQS SIPYREEL
//