YDR09_YEAST
ID YDR09_YEAST Reviewed; 715 AA.
AC Q04585; D6VS95;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=D-ribulokinase YDR109C;
DE EC=2.7.1.47 {ECO:0000269|PubMed:27909055};
GN OrderedLocusNames=YDR109C {ECO:0000303|PubMed:27909055,
GN ECO:0000312|SGD:S000002516};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=27909055; DOI=10.1074/jbc.m116.760744;
RA Singh C., Glaab E., Linster C.L.;
RT "Molecular Identification of d-Ribulokinase in Budding Yeast and Mammals.";
RL J. Biol. Chem. 292:1005-1028(2017).
CC -!- FUNCTION: Catalyzes ATP-dependent phosphorylation of D-ribulose at C-5
CC to form D-ribulose 5-phosphate. Postulated to function in a metabolite
CC repair mechanism by preventing toxic accumulation of free D-ribulose
CC formed by non-specific phosphatase activities. Alternatively, may play
CC a role in regulating D-ribulose 5-phosphate recycling in the pentose
CC phosphate pathway. {ECO:0000269|PubMed:27909055}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+);
CC Xref=Rhea:RHEA:17601, ChEBI:CHEBI:15378, ChEBI:CHEBI:17173,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58121, ChEBI:CHEBI:456216;
CC EC=2.7.1.47; Evidence={ECO:0000269|PubMed:27909055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17602;
CC Evidence={ECO:0000305|PubMed:27909055};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=217 uM for D-ribulose {ECO:0000269|PubMed:27909055};
CC Vmax=22 umol/min/mg enzyme toward D-ribulose
CC {ECO:0000269|PubMed:27909055};
CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC interconversion. {ECO:0000305|PubMed:27909055}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
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DR EMBL; Z48758; CAA88663.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11955.1; -; Genomic_DNA.
DR PIR; S52675; S52675.
DR RefSeq; NP_010394.3; NM_001180417.3.
DR AlphaFoldDB; Q04585; -.
DR SMR; Q04585; -.
DR BioGRID; 32167; 19.
DR STRING; 4932.YDR109C; -.
DR iPTMnet; Q04585; -.
DR MaxQB; Q04585; -.
DR PaxDb; Q04585; -.
DR PRIDE; Q04585; -.
DR EnsemblFungi; YDR109C_mRNA; YDR109C; YDR109C.
DR GeneID; 851687; -.
DR KEGG; sce:YDR109C; -.
DR SGD; S000002516; YDR109C.
DR VEuPathDB; FungiDB:YDR109C; -.
DR eggNOG; KOG2517; Eukaryota.
DR GeneTree; ENSGT01000000214434; -.
DR HOGENOM; CLU_009281_10_1_1; -.
DR InParanoid; Q04585; -.
DR OMA; GHKAMWH; -.
DR BioCyc; MetaCyc:G3O-29711-MON; -.
DR BioCyc; YEAST:G3O-29711-MON; -.
DR BRENDA; 2.7.1.47; 984.
DR UniPathway; UPA00246; -.
DR PRO; PR:Q04585; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04585; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0019150; F:D-ribulokinase activity; IDA:SGD.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IBA:GO_Central.
DR GO; GO:0019321; P:pentose metabolic process; IDA:SGD.
DR CDD; cd07782; FGGY_YpCarbK_like; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR006003; FGGY_RbtK-like.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01315; 5C_CHO_kinase; 1.
PE 1: Evidence at protein level;
KW Kinase; Reference proteome; Transferase.
FT CHAIN 1..715
FT /note="D-ribulokinase YDR109C"
FT /id="PRO_0000244445"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 715 AA; 79161 MW; A52B2D9B4B4C9C7E CRC64;
MKSRKRQNNM QNETREPAVL SSQETSISRI SPQDPEAKFY VGVDVGTGSA RACVIDQSGN
MLSLAEKPIK REQLISNFIT QSSREIWNAV CYCVRTVVEE SGVDPERVRG IGFDATCSLV
VVSATNFEEI AVGPDFTNND QNIILWMDHR AMKETEEINS SGDKCLKYVG GQMSVEMEIP
KIKWLKNNLE AGIFQDCKFF DLPDYLTFKA TGKENRSFCS AVCKQGFLPV GVEGSDIGWS
KEFLNSIGLS ELTKNDFERL GGSLREKKNF LTAGECISPL DKKAACQLGL TEHCVVSSGI
IDAYAGWVGT VAAKPESAVK GLAETENYKK DFNGAIGRLA AVAGTSTCHI LLSKNPIFVH
GVWGPYRDVL ARGFWAAEGG QSCTGVLLDH LITTHPAFTE LSHMANLAGV SKFEYLNKIL
ETLVEKRKVR SVISLAKHLF FYGDYHGNRS PIADPNMRAC IIGQSMDNSI EDLAVMYLSA
CEFISQQTRQ IIEVMLKSGH EINAIFMSGG QCRNSLLMRL LADCTGLPIV IPRYVDAAVV
FGSALLGAAA SEDFDYTREK RTLKGQKSSQ TKTERFNDSY SSIQKLSMED RNSTNGFVSP
HNLQLSTPSA PAKINNYSLP ICTQQPLDKT SEESSKDASL TVGQESLGEG RYNGTSFLWK
VMQELTGNAR IVNPNEKTHP DRILLDTKYQ IFLDMIETQR KYRRMVDKVE GSFSR
