ID   RBSK_YEAST              Reviewed;         333 AA.
AC   P25332; D6VR46;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 2.
DT   04-NOV-2026, entry version 190.
DE   RecName: Full=Ribokinase {ECO:0000255|HAMAP-Rule:MF_03215, ECO:0000303|PubMed:1964349};
DE            Short=RK {ECO:0000255|HAMAP-Rule:MF_03215};
DE            EC=2.7.1.15 {ECO:0000250|UniProtKB:P0A9J6, ECO:0000255|HAMAP-Rule:MF_03215};
GN   Name=RBK1 {ECO:0000255|HAMAP-Rule:MF_03215,
GN   ECO:0000303|PubMed:1964349};
GN   OrderedLocusNames=YCR036W {ECO:0000312|SGD:S000000632};
GN   ORFNames=YCR36W, YCR523;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=1964349; DOI=10.1002/yea.320060609;
RA   Thierry A., Fairhead C., Dujon B.;
RT   "The complete sequence of the 8.2 kb segment left of MAT on chromosome III
RT   reveals five ORFs, including a gene for a yeast ribokinase.";
RL   Yeast 6:521-534(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
RN   [3]
RP   SEQUENCE REVISION TO 178 AND 301.
RA   Valles G., Volckaerts G.;
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
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=D-ribose + ATP = D-ribose 5-phosphate + ADP + 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; Evidence={ECO:0000255|HAMAP-
CC         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       ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03215,
CC       ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 1780 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. Ribokinase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03215}.
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DR   EMBL; X56909; CAA40228.1; -; Genomic_DNA.
DR   EMBL; X59720; CAA42303.2; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07515.1; -; Genomic_DNA.
DR   PIR; S12918; KIBYRB.
DR   RefSeq; NP_009965.2; NM_001178750.1.
DR   PDB; 9M8T; X-ray; 2.66 A; A/B=1-333.
DR   PDB; 9U3W; X-ray; 2.91 A; A/B=1-333.
DR   AlphaFoldDB; P25332; -.
DR   SMR; P25332; -.
DR   BioGRID; 31019; 147.
DR   DIP; DIP-4990N; -.
DR   FunCoup; P25332; 1337.
DR   IntAct; P25332; 24.
DR   STRING; 4932.YCR036W; -.
DR   GlyGen; P25332; 5 sites, 1 O-linked glycan (5 sites).
DR   PaxDb; 4932-YCR036W; -.
DR   PeptideAtlas; P25332; -.
DR   EnsemblFungi; YCR036W_mRNA; YCR036W; YCR036W.
DR   GeneID; 850402; -.
DR   KEGG; sce:YCR036W; -.
DR   AGR; SGD:S000000632; -.
DR   SGD; S000000632; RBK1.
DR   VEuPathDB; FungiDB:YCR036W; -.
DR   eggNOG; KOG2855; Eukaryota.
DR   HOGENOM; CLU_027634_2_0_1; -.
DR   InParanoid; P25332; -.
DR   OMA; AAEHLIM; -.
DR   OrthoDB; 415590at2759; -.
DR   BioCyc; YEAST:YCR036W-MONOMER; -.
DR   UniPathway; UPA00916; UER00889.
DR   BioGRID-ORCS; 850402; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P25332; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25332; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004747; F:ribokinase activity; IDA:SGD.
DR   GO; GO:0046835; P:carbohydrate phosphorylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0019303; P:D-ribose catabolic process; IMP:SGD.
DR   CDD; cd01174; ribokinase; 1.
DR   FunFam; 3.40.1190.20:FF:000071; 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; IPR011611; PfkB_dom.
DR   InterPro; IPR002139; Ribo/fructo_kinase.
DR   InterPro; IPR011877; Ribokinase.
DR   InterPro; IPR029056; Ribokinase-like.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Carbohydrate metabolism; Cytoplasm; Kinase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Potassium;
KW   Reference proteome; Transferase.
FT   CHAIN           1..333
FT                   /note="Ribokinase"
FT                   /id="PRO_0000080094"
FT   ACT_SITE        283
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         10..12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         38..42
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         193
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         248..253
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         277
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         279
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         282..283
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         283
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         313
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         316
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         318
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         322
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   CONFLICT        178
FT                   /note="A -> T (in Ref. 1; CAA40228)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        301
FT                   /note="T -> M (in Ref. 1; CAA40228)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   333 AA;  36924 MW;  226B44DA7E458B95 CRC64;
     MGITVIGSLN YDLDTFTDRL PNAGETFRAN HFETHAGGKG LNQAAAIGKL KNPSSRYSVR
     MIGNVGNDTF GKQLKDTLSD CGVDITHVGT YEGINTGTAT ILIEEKAGGQ NRILIVEGAN
     SKTIYDPKQL CEIFPEGKEE EEYVVFQHEI PDPLSIIKWI HANRPNFQIV YNPSPFKAMP
     KKDWELVDLL VVNEIEGLQI VESVFDNELV EEIREKIKDD FLGEYRKICE LLYEKLMNRK
     KRGIVVMTLG SRGVLFCSHE SPEVQFLPAI QNVSVVDTTG AGDTFLGGLV TQLYQGETLS
     TAIKFSTLAS SLTIQRKGAA ESMPLYKDVQ KDA
//