RBSK_MOUSE
ID RBSK_MOUSE Reviewed; 323 AA.
AC Q8R1Q9;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ribokinase {ECO:0000255|HAMAP-Rule:MF_03215, ECO:0000312|EMBL:AAH23339.1};
DE Short=RK {ECO:0000255|HAMAP-Rule:MF_03215};
DE EC=2.7.1.15 {ECO:0000255|HAMAP-Rule:MF_03215};
GN Name=Rbks {ECO:0000255|HAMAP-Rule:MF_03215, ECO:0000312|EMBL:AAH23339.1,
GN ECO:0000312|MGI:MGI:1918586}; Synonyms=Rbsk {ECO:0000250|UniProtKB:Q9H477};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:BAE23825.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE23825.1};
RC TISSUE=Aorta {ECO:0000312|EMBL:BAE23825.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2] {ECO:0000312|EMBL:AAH23339.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH23339.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Competitively inhibited by phosphonoacetic
CC acid, etidronate, 2-carboxethylphosphonic acid, N-
CC (phosphonomethyl)glycine, N-(phosphonomethyl)iminodiacetic acid and
CC clodronate (By similarity). {ECO:0000250|UniProtKB:Q9H477,
CC 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; AK138939; BAE23825.1; -; mRNA.
DR EMBL; BC023339; AAH23339.1; -; mRNA.
DR CCDS; CCDS19187.1; -.
DR RefSeq; NP_694876.1; NM_153196.1.
DR AlphaFoldDB; Q8R1Q9; -.
DR SMR; Q8R1Q9; -.
DR STRING; 10090.ENSMUSP00000031018; -.
DR iPTMnet; Q8R1Q9; -.
DR PhosphoSitePlus; Q8R1Q9; -.
DR EPD; Q8R1Q9; -.
DR MaxQB; Q8R1Q9; -.
DR PaxDb; Q8R1Q9; -.
DR PeptideAtlas; Q8R1Q9; -.
DR PRIDE; Q8R1Q9; -.
DR ProteomicsDB; 255162; -.
DR Antibodypedia; 13898; 141 antibodies from 21 providers.
DR DNASU; 71336; -.
DR Ensembl; ENSMUST00000031018; ENSMUSP00000031018; ENSMUSG00000029136.
DR GeneID; 71336; -.
DR KEGG; mmu:71336; -.
DR UCSC; uc008wyv.1; mouse.
DR CTD; 64080; -.
DR MGI; MGI:1918586; Rbks.
DR VEuPathDB; HostDB:ENSMUSG00000029136; -.
DR eggNOG; KOG2855; Eukaryota.
DR GeneTree; ENSGT00390000005743; -.
DR HOGENOM; CLU_027634_2_3_1; -.
DR InParanoid; Q8R1Q9; -.
DR OMA; IPWRDEL; -.
DR OrthoDB; 918144at2759; -.
DR PhylomeDB; Q8R1Q9; -.
DR TreeFam; TF105770; -.
DR Reactome; R-MMU-71336; Pentose phosphate pathway.
DR UniPathway; UPA00916; UER00889.
DR BioGRID-ORCS; 71336; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Rbks; mouse.
DR PRO; PR:Q8R1Q9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8R1Q9; protein.
DR Bgee; ENSMUSG00000029136; Expressed in lumbar dorsal root ganglion and 127 other tissues.
DR Genevisible; Q8R1Q9; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004747; F:ribokinase activity; IMP:MGI.
DR GO; GO:0019303; P:D-ribose catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006098; P:pentose-phosphate shunt; IDA:MGI.
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; PS00584; PFKB_KINASES_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Cytoplasm; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleus; Potassium; Reference proteome;
KW Transferase.
FT CHAIN 1..323
FT /note="Ribokinase"
FT /id="PRO_0000375977"
FT ACT_SITE 270
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 26..28
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 54..58
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 236..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 257
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 296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 302
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 305
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 307
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT BINDING 311
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
SQ SEQUENCE 323 AA; 34119 MW; 65A93A8372651F60 CRC64;
MAACGEPGRP WQEEEAAAVV VVGSCMTDLV SLTSRLPKTG ETIHGHEFFI GFGGKGANQC
VQAARLGAKA AIVCKVGNDS FGNDYIENLK QNHISTEFTY QTRDAATGTA SIIVNNEGQN
IIVIVAGANL FLNSEDLKKA ASVISRAKVM ICQLEISPAA SLEALTMARR SGVKTLFNPA
PAMADLDPQF YTLSSIFCCN ESEAEILTGH AVSDPTTAGK AAMILLERGC QVVVITLGAS
GCVILSQAEP VPKHIPTEAV KAVDTTGAGD SFVGALAFYL AYYPNLSLEE MLKRSNFIAA
VSVQATGTQS SYPYKKDLPL ALF
