ID XYLB_MOUSE Reviewed; 551 AA.
AC Q3TNA1; B2RR66; Q8R156;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=Xylulose kinase;
DE Short=Xylulokinase;
DE EC=2.7.1.17;
GN Name=Xylb;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, and Kidney;
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, and Liver;
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: Phosphorylates D-xylulose to produce D-xylulose 5-phosphate,
CC a molecule that may play an important role in the regulation of glucose
CC metabolism and lipogenesis. {ECO:0000250}.
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;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25442.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK143476; BAE25393.1; -; mRNA.
DR EMBL; AK165440; BAE38188.1; -; mRNA.
DR EMBL; AK165518; BAE38233.1; -; mRNA.
DR EMBL; BC025442; AAH25442.1; ALT_INIT; mRNA.
DR EMBL; BC138244; AAI38245.1; -; mRNA.
DR EMBL; BC138247; AAI38248.1; -; mRNA.
DR CCDS; CCDS23614.1; -.
DR RefSeq; NP_001028381.1; NM_001033209.3.
DR RefSeq; NP_001186497.1; NM_001199568.1.
DR AlphaFoldDB; Q3TNA1; -.
DR SMR; Q3TNA1; -.
DR BioGRID; 221878; 5.
DR STRING; 10090.ENSMUSP00000047254; -.
DR iPTMnet; Q3TNA1; -.
DR PhosphoSitePlus; Q3TNA1; -.
DR SwissPalm; Q3TNA1; -.
DR jPOST; Q3TNA1; -.
DR MaxQB; Q3TNA1; -.
DR PaxDb; 10090-ENSMUSP00000047254; -.
DR PeptideAtlas; Q3TNA1; -.
DR ProteomicsDB; 297656; -.
DR Pumba; Q3TNA1; -.
DR Antibodypedia; 28592; 85 antibodies from 19 providers.
DR DNASU; 102448; -.
DR Ensembl; ENSMUST00000039610.10; ENSMUSP00000047254.9; ENSMUSG00000035769.10.
DR GeneID; 102448; -.
DR KEGG; mmu:102448; -.
DR UCSC; uc009sat.2; mouse.
DR AGR; MGI:2142985; -.
DR CTD; 9942; -.
DR MGI; MGI:2142985; Xylb.
DR VEuPathDB; HostDB:ENSMUSG00000035769; -.
DR eggNOG; KOG2531; Eukaryota.
DR GeneTree; ENSGT01000000214434; -.
DR HOGENOM; CLU_016149_8_0_1; -.
DR InParanoid; Q3TNA1; -.
DR OMA; STHFFNH; -.
DR OrthoDB; 1704034at2759; -.
DR PhylomeDB; Q3TNA1; -.
DR TreeFam; TF313643; -.
DR Reactome; R-MMU-5661270; Formation of xylulose-5-phosphate.
DR BioGRID-ORCS; 102448; 4 hits in 79 CRISPR screens.
DR ChiTaRS; Xylb; mouse.
DR PRO; PR:Q3TNA1; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q3TNA1; Protein.
DR Bgee; ENSMUSG00000035769; Expressed in right kidney and 154 other cell types or tissues.
DR ExpressionAtlas; Q3TNA1; baseline and differential.
DR Genevisible; Q3TNA1; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004856; F:xylulokinase activity; ISS:UniProtKB.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019640; P:glucuronate catabolic process to xylulose 5-phosphate; ISO:MGI.
DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR GO; GO:0005997; P:xylulose metabolic process; ISS:UniProtKB.
DR CDD; cd07776; FGGY_D-XK_euk; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR042024; D-XK_euk.
DR InterPro; IPR018485; FGGY_C.
DR InterPro; IPR018484; FGGY_N.
DR PANTHER; PTHR10196; SUGAR KINASE; 1.
DR PANTHER; PTHR10196:SF57; XYLULOSE KINASE; 1.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase; Xylose metabolism.
FT CHAIN 1..551
FT /note="Xylulose kinase"
FT /id="PRO_0000230986"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 456..457
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 551 AA; 59544 MW; CED895069FBFD97B CRC64;
MDARTHRRAA GTPRALAERA GRRCCLGWDF STQQVKVVAV DAELNVFYED SVHFDRDLPE
FGTQGGVHVH KDRLTVTSPV LMWVQALDLI LGKMKSSGFD FSQVLALSGA GQQHGSVYWK
TGASLALSSL SPALPLHQQL QSCFSISDCP IWMDSSTTAQ CHQLEAAVGG AQALSCLTGS
RAYERFTGNQ IAKLFQKNPE AYSHSERISL VSSFAASLFL GGYSPIDYSD GSGMNLLQIQ
EKVWSQACLD VCAPHLEEKL GSPVPSCSVV GTISSYYVQR YGFPPGCKVV AFSGDNPASL
AGMRLEEGDI AVSLGTSDTL FLWLQKPMPA LEGHIFCNPV DPQHYMALLC FKNGSLMREK
IRDESASCSW NKFSKALKST AMGNNGNLGF YFDVMEITPE IIGRHRFNAE NMEVSAFPGD
VEIRALIEGQ FMAKRIHAEG LGYRVMPKTK ILATGGASHN KDILQVLADV FGAPVYVIDT
TSSACVGSAY RAFHGLAGGT GVAFSEVVKS APQPSLAATP NPGASQVYAA LLPRYSALEQ
RILSTAQRPL E
//
