ID E3DLT0_HALPG Unreviewed; 305 AA.
AC E3DLT0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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 OrderedLocusNames=Hprae_1126 {ECO:0000313|EMBL:ADO77277.1};
OS Halanaerobium praevalens (strain ATCC 33744 / DSM 2228 / GSL).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halanaerobium.
OX NCBI_TaxID=572479 {ECO:0000313|EMBL:ADO77277.1, ECO:0000313|Proteomes:UP000006866};
RN [1] {ECO:0000313|Proteomes:UP000006866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33744 / DSM 2228 / GSL
RC {ECO:0000313|Proteomes:UP000006866};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Chertkov O., Detter J.C., Han C., Larimer F., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Tindall B., Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Halanaerobium praevalens DSM 2228.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO77277.1, ECO:0000313|Proteomes:UP000006866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33744 / DSM 2228 / GSL
RC {ECO:0000313|Proteomes:UP000006866};
RX PubMed=21886858;
RA Ivanova N., Sikorski J., Chertkov O., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Huntemann M., Liolios K., Pagani I., Mavromatis K., Ovchinikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M.,
RA Kannan K.P., Rohde M., Tindall B.J., Goker M., Detter J.C., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Lapidus A.;
RT "Complete genome sequence of the extremely halophilic Halanaerobium
RT praevalens type strain (GSL).";
RL Stand. Genomic Sci. 4:312-321(2011).
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 -!- 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; CP002175; ADO77277.1; -; Genomic_DNA.
DR RefSeq; WP_014553307.1; NC_017455.1.
DR AlphaFoldDB; E3DLT0; -.
DR STRING; 572479.Hprae_1126; -.
DR KEGG; hpk:Hprae_1126; -.
DR PATRIC; fig|572479.3.peg.1138; -.
DR eggNOG; COG0524; Bacteria.
DR HOGENOM; CLU_027634_2_0_9; -.
DR OrthoDB; 9775849at2; -.
DR UniPathway; UPA00916; UER00889.
DR Proteomes; UP000006866; 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 Reference proteome {ECO:0000313|Proteomes:UP000006866};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01987}.
FT DOMAIN 1..292
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
FT ACT_SITE 250
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 11..13
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 39..43
FT /ligand="substrate"
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 218..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 244
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
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 249..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 280
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 283
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 289
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
SQ SEQUENCE 305 AA; 32503 MW; 29BACA522C838EF8 CRC64;
MSKILVIGSM NMDLVVQTER YPEAGETIIG GKFAQIPGGK GANQALAAAK LGDEVQFIGA
CGDDSFAPML KSSLKNGGAK IDNIFEIKDK STGVAVITVD PEGNNRIIVS PGANYELDLA
KIEKIKSQII EAEIILLQLE IPVETIAKIV EIAAANNTKI ILDPAPAQQL SDHILSEIDF
LLPNEGELDL LMAAADAKTR SEKIEILLDK GVKNIIVTEG EKGLNFYNKE QALHLDALKV
KAVDTTAAGD VFAGAFAASL ISENDLEKSL KCAVQAAAYS VSKRGAQSSI PDQNELNEFL
AERSN
//