ID Q22KI6_TETTS Unreviewed; 337 AA. AC Q22KI6; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 2. DT 27-MAR-2024, entry version 77. DE RecName: Full=Ribokinase {ECO:0000256|ARBA:ARBA00016943, ECO:0000256|HAMAP-Rule:MF_03215}; DE Short=RK {ECO:0000256|HAMAP-Rule:MF_03215}; DE EC=2.7.1.15 {ECO:0000256|ARBA:ARBA00012035, ECO:0000256|HAMAP-Rule:MF_03215}; GN ORFNames=TTHERM_00312950 {ECO:0000313|EMBL:EAR85813.2}; OS Tetrahymena thermophila (strain SB210). OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae; OC Tetrahymena. OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR85813.2, ECO:0000313|Proteomes:UP000009168}; RN [1] {ECO:0000313|Proteomes:UP000009168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168}; RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286; RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R., RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L., RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M., RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L., RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y., RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z., RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A., RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A., RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A., RA Hamilton E.P., Orias E.; RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a RT model eukaryote."; RL PLoS Biol. 4:1620-1642(2006). 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_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:0000256|ARBA:ARBA00000691, CC ECO:0000256|HAMAP-Rule:MF_03215}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_03215}. 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_03215}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03215}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03215}. CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03215}. CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. Ribokinase CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03215}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03215}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GG662498; EAR85813.2; -; Genomic_DNA. DR RefSeq; XP_001033476.2; XM_001033476.3. DR AlphaFoldDB; Q22KI6; -. DR STRING; 312017.Q22KI6; -. DR EnsemblProtists; EAR85813; EAR85813; TTHERM_00312950. DR GeneID; 7825277; -. DR KEGG; tet:TTHERM_00312950; -. DR eggNOG; KOG2855; Eukaryota. DR HOGENOM; CLU_027634_2_0_1; -. DR InParanoid; Q22KI6; -. DR OMA; DIVLIQQ; -. DR OrthoDB; 5475204at2759; -. DR UniPathway; UPA00916; UER00889. DR Proteomes; UP000009168; Unassembled WGS sequence. 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 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. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03215}; KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_03215}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03215}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_03215, ECO:0000313|EMBL:EAR85813.2}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03215}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03215}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03215}; KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03215}; KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_03215}; KW Reference proteome {ECO:0000313|Proteomes:UP000009168}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03215}. FT DOMAIN 7..325 FT /note="Carbohydrate kinase PfkB" FT /evidence="ECO:0000259|Pfam:PF00294" FT ACT_SITE 271 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 15..17 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 43..47 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 146 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 191 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 230..235 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 265 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 267 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 270..271 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 271 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 307 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 313 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 316 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 318 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 322 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" SQ SEQUENCE 337 AA; 36861 MW; DAD052BA8A22BE1E CRC64; MAQNTYSICV VGSGSFDLFL LVNHFPVEGE TLQANDSFIK NGGKGANQAV AAAKLGAKTI FAGQFGQDKY GDGLVEEMSQ SGVDMSKVRR LANVQTGQAI ITLNKKGENS IIIVGGANTH YDHLNVLPQE FKDAIQSSRI ILLQKEIPLE ISKLAAIYAK QHNKLVMLDC GGRDEDIPEE LLQNIDFISP NQSELKRVMN INSSDHGEIT IDEIRQQLLS KYPNLTVVLK EGSKGSAVIT KTDYLHVDSA SLIKPDILNT YKIVDTTGAG DCFTAAFCVE FDKLFPQNGV QYEDALEKYK KCLLFANCSA FVCITVMGAM PSMPKLESVQ QLLSKVQ //