XKS1_YEAST
ID XKS1_YEAST Reviewed; 600 AA.
AC P42826; D6VUX6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Xylulose kinase {ECO:0000303|PubMed:9595677};
DE Short=Xylulokinase {ECO:0000303|PubMed:9595677};
DE EC=2.7.1.17 {ECO:0000305|PubMed:9595677};
GN Name=XKS1 {ECO:0000303|PubMed:9595677}; OrderedLocusNames=YGR194C;
GN ORFNames=G7584;
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-502.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7645350; DOI=10.1002/yea.320110609;
RA Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez M., Nombela C.;
RT "The complete sequence of a 9037 bp DNA fragment of the right arm of
RT Saccharomyces cerevisiae chromosome VII.";
RL Yeast 11:587-591(1995).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9595677; DOI=10.1111/j.1574-6968.1998.tb12993.x;
RA Rodriguez-Pena J.M., Cid V.J., Arroyo J., Nombela C.;
RT "The YGR194c (XKS1) gene encodes the xylulokinase from the budding yeast
RT Saccharomyces cerevisiae.";
RL FEMS Microbiol. Lett. 162:155-160(1998).
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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Xylulose kinase necessary for growth in culture media with D-
CC xylulose as the solecarbon source. {ECO:0000269|PubMed:9595677}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-xylulose = ADP + D-xylulose 5-phosphate + H(+);
CC Xref=Rhea:RHEA:10964, ChEBI:CHEBI:15378, ChEBI:CHEBI:17140,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57737, ChEBI:CHEBI:456216;
CC EC=2.7.1.17; Evidence={ECO:0000305|PubMed:9595677};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Impairs growth in culture media with D-xylulose
CC as the sole carbon source. {ECO:0000269|PubMed:9595677}.
CC -!- MISCELLANEOUS: Present with 3460 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
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; Z72979; CAA97220.1; -; Genomic_DNA.
DR EMBL; X82408; CAA57805.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08287.1; -; Genomic_DNA.
DR PIR; S64512; S64512.
DR RefSeq; NP_011710.3; NM_001181323.3.
DR AlphaFoldDB; P42826; -.
DR SMR; P42826; -.
DR BioGRID; 33447; 93.
DR DIP; DIP-6764N; -.
DR IntAct; P42826; 2.
DR STRING; 4932.YGR194C; -.
DR iPTMnet; P42826; -.
DR MaxQB; P42826; -.
DR PaxDb; P42826; -.
DR PRIDE; P42826; -.
DR EnsemblFungi; YGR194C_mRNA; YGR194C; YGR194C.
DR GeneID; 853108; -.
DR KEGG; sce:YGR194C; -.
DR SGD; S000003426; XKS1.
DR VEuPathDB; FungiDB:YGR194C; -.
DR eggNOG; KOG2531; Eukaryota.
DR GeneTree; ENSGT01000000214434; -.
DR HOGENOM; CLU_016149_5_0_1; -.
DR InParanoid; P42826; -.
DR OMA; QHGTVFW; -.
DR BioCyc; YEAST:YGR194C-MON; -.
DR BRENDA; 2.7.1.17; 984.
DR Reactome; R-SCE-5661270; Formation of xylulose-5-phosphate.
DR PRO; PR:P42826; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P42826; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
DR GO; GO:0004856; F:xylulokinase activity; IMP:SGD.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR GO; GO:0005998; P:xylulose catabolic process; IDA:SGD.
DR GO; GO:0005997; P:xylulose metabolic process; IBA:GO_Central.
DR CDD; cd07776; FGGY_D-XK_euk; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR042024; D-XK_euk.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Cytoplasm; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Xylose metabolism.
FT CHAIN 1..600
FT /note="Xylulose kinase"
FT /id="PRO_0000059563"
FT BINDING 79..82
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q31KC7"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q31KC7"
FT BINDING 358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8L794"
FT BINDING 505..509
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8L794"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 497..502
FT /note="PERTFF -> QKGLFL (in Ref. 3; CAA57805)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 600 AA; 68321 MW; 29A7DC28F92AA527 CRC64;
MLCSVIQRQT REVSNTMSLD SYYLGFDLST QQLKCLAINQ DLKIVHSETV EFEKDLPHYH
TKKGVYIHGD TIECPVAMWL EALDLVLSKY REAKFPLNKV MAVSGSCQQH GSVYWSSQAE
SLLEQLNKKP EKDLLHYVSS VAFARQTAPN WQDHSTAKQC QEFEECIGGP EKMAQLTGSR
AHFRFTGPQI LKIAQLEPEA YEKTKTISLV SNFLTSILVG HLVELEEADA CGMNLYDIRE
RKFSDELLHL IDSSSKDKTI RQKLMRAPMK NLIAGTICKY FIEKYGFNTN CKVSPMTGDN
LATICSLPLR KNDVLVSLGT STTVLLVTDK YHPSPNYHLF IHPTLPNHYM GMICYCNGSL
ARERIRDELN KERENNYEKT NDWTLFNQAV LDDSESSENE LGVYFPLGEI VPSVKAINKR
VIFNPKTGMI EREVAKFKDK RHDAKNIVES QALSCRVRIS PLLSDSNASS QQRLNEDTIV
KFDYDESPLR DYLNKRPERT FFVGGASKND AIVKKFAQVI GATKGNFRLE TPNSCALGGC
YKAMWSLLYD SNKIAVPFDK FLNDNFPWHV MESISDVDNE NWDRYNSKIV PLSELEKTLI
