RBSK_DICDI
ID RBSK_DICDI Reviewed; 318 AA.
AC Q54UQ4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Ribokinase {ECO:0000255|HAMAP-Rule:MF_03215};
DE Short=RK {ECO:0000255|HAMAP-Rule:MF_03215};
DE EC=2.7.1.15 {ECO:0000255|HAMAP-Rule:MF_03215};
GN Name=rbsk; ORFNames=DDB_G0280893;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(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:0000255|HAMAP-Rule:MF_03215}.
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_03215};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03215};
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_03215};
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_03215}.
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_03215}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03215}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03215}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03215}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. Ribokinase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03215}.
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DR EMBL; AAFI02000039; EAL66988.2; -; Genomic_DNA.
DR RefSeq; XP_640967.2; XM_635875.2.
DR AlphaFoldDB; Q54UQ4; -.
DR SMR; Q54UQ4; -.
DR STRING; 44689.DDB0304695; -.
DR PaxDb; Q54UQ4; -.
DR PRIDE; Q54UQ4; -.
DR EnsemblProtists; EAL66988; EAL66988; DDB_G0280893.
DR GeneID; 8622771; -.
DR KEGG; ddi:DDB_G0280893; -.
DR dictyBase; DDB_G0280893; rbsk.
DR eggNOG; KOG2855; Eukaryota.
DR HOGENOM; CLU_027634_2_3_1; -.
DR InParanoid; Q54UQ4; -.
DR OMA; IPWRDEL; -.
DR PhylomeDB; Q54UQ4; -.
DR Reactome; R-DDI-71336; Pentose phosphate pathway.
DR UniPathway; UPA00916; UER00889.
DR PRO; PR:Q54UQ4; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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; Carbohydrate metabolism; Cytoplasm; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleus; Potassium; Reference proteome;
KW Transferase.
FT CHAIN 1..318
FT /note="Ribokinase"
FT /id="PRO_0000328525"
FT ACT_SITE 270
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 12..14
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 40..44
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 235..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 264
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 266
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 269..270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 301
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 304
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 306
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 310
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
SQ SEQUENCE 318 AA; 34811 MW; 94BFCDB060FCA201 CRC64;
MENNITVVGA SNWDTFIYVD KMPRVGETIK GTDLKVSYGG KAANQAVQAS LLGSNCTLIT
KLGDDPSGVN TLKNFKDKNI NCEFVSVVSN VPSGCATIIV DKNGDNNIII IGGSNDLLNE
KDVDNAKSQI QNSSLLLCQL EVSLNVTLHA LKIAKESNKC KTMLNLTPIN NDPLILEMFK
FVDILIVNEI ELIGLYNSTF NNNNNNEKDF NINQLMEMCD NLIKKFENFE NIIVTLGGNG
QLLVSKENNK NCHIELKEKV KVVDTSGAGD SFIGSFAHYL VTENKPLKDS IESASKVASI
SVTRHGTQTS YPKSNEIN
