ID XYLB_HUMAN Reviewed; 536 AA. AC O75191; B2RAW4; B4DDT2; B9EH64; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 3. DT 27-MAR-2024, entry version 153. DE RecName: Full=Xylulose kinase; DE Short=Xylulokinase; DE EC=2.7.1.17; GN Name=XYLB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP GLU-85. RC TISSUE=Kidney, and Mammary gland; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-85. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung, and Testis; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-512 (ISOFORM 1), AND VARIANTS GLU-85 AND RP ASN-262. RC TISSUE=Liver; RX PubMed=9763671; DOI=10.1159/000015076; RA Tamari M., Daigo Y., Ishikawa S., Nakamura Y.; RT "Genomic structure of a novel human gene (XYLB) on chromosome 3p22-->p21.3 RT encoding a xylulokinase-like protein."; RL Cytogenet. Cell Genet. 82:101-104(1998). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) IN COMPLEX WITH D-XYLULOSE AND ADP, RP CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=23179721; DOI=10.1074/jbc.m112.427997; RA Bunker R.D., Bulloch E.M., Dickson J.M., Loomes K.M., Baker E.N.; RT "Structure and function of human xylulokinase, an enzyme with important RT roles in carbohydrate metabolism."; RL J. Biol. Chem. 288:1643-1652(2013). 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:0000269|PubMed:23179721}. 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:0000269|PubMed:23179721}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=24 uM for D-xylulose {ECO:0000269|PubMed:23179721}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23179721}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O75191-1; Sequence=Displayed; CC Name=2; CC IsoId=O75191-2; Sequence=VSP_055522; CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA31527.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={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; AK293325; BAG56843.1; -; mRNA. DR EMBL; AK314386; BAG37011.1; -; mRNA. DR EMBL; AP006191; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP006193; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW64532.1; -; Genomic_DNA. DR EMBL; BC137076; AAI37077.1; -; mRNA. DR EMBL; BC137080; AAI37081.1; -; mRNA. DR EMBL; AB015046; BAA31527.1; ALT_SEQ; mRNA. DR CCDS; CCDS2678.1; -. [O75191-1] DR RefSeq; NP_005099.2; NM_005108.3. [O75191-1] DR PDB; 4BC2; X-ray; 1.97 A; A/B/C=1-536. DR PDB; 4BC3; X-ray; 1.68 A; A/B/C=1-536. DR PDB; 4BC4; X-ray; 1.79 A; A/B/C=1-536. DR PDB; 4BC5; X-ray; 1.98 A; A/B/C=1-536. DR PDBsum; 4BC2; -. DR PDBsum; 4BC3; -. DR PDBsum; 4BC4; -. DR PDBsum; 4BC5; -. DR AlphaFoldDB; O75191; -. DR SMR; O75191; -. DR BioGRID; 115268; 14. DR IntAct; O75191; 1. DR STRING; 9606.ENSP00000207870; -. DR iPTMnet; O75191; -. DR MetOSite; O75191; -. DR PhosphoSitePlus; O75191; -. DR BioMuta; XYLB; -. DR EPD; O75191; -. DR jPOST; O75191; -. DR MassIVE; O75191; -. DR MaxQB; O75191; -. DR PaxDb; 9606-ENSP00000207870; -. DR PeptideAtlas; O75191; -. DR ProteomicsDB; 3889; -. DR ProteomicsDB; 49863; -. [O75191-1] DR Pumba; O75191; -. DR Antibodypedia; 28592; 85 antibodies from 19 providers. DR DNASU; 9942; -. DR Ensembl; ENST00000207870.8; ENSP00000207870.3; ENSG00000093217.11. [O75191-1] DR GeneID; 9942; -. DR KEGG; hsa:9942; -. DR MANE-Select; ENST00000207870.8; ENSP00000207870.3; NM_005108.4; NP_005099.2. DR UCSC; uc003cic.3; human. [O75191-1] DR AGR; HGNC:12839; -. DR CTD; 9942; -. DR DisGeNET; 9942; -. DR GeneCards; XYLB; -. DR HGNC; HGNC:12839; XYLB. DR HPA; ENSG00000093217; Tissue enhanced (liver). DR MIM; 604049; gene. DR neXtProt; NX_O75191; -. DR OpenTargets; ENSG00000093217; -. DR PharmGKB; PA37430; -. DR VEuPathDB; HostDB:ENSG00000093217; -. DR eggNOG; KOG2531; Eukaryota. DR GeneTree; ENSGT01000000214434; -. DR HOGENOM; CLU_016149_8_0_1; -. DR InParanoid; O75191; -. DR OMA; STHFFNH; -. DR OrthoDB; 1704034at2759; -. DR PhylomeDB; O75191; -. DR TreeFam; TF313643; -. DR BRENDA; 2.7.1.17; 2681. DR PathwayCommons; O75191; -. DR Reactome; R-HSA-5661270; Formation of xylulose-5-phosphate. DR BioGRID-ORCS; 9942; 13 hits in 1161 CRISPR screens. DR ChiTaRS; XYLB; human. DR GenomeRNAi; 9942; -. DR Pharos; O75191; Tbio. DR PRO; PR:O75191; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; O75191; Protein. DR Bgee; ENSG00000093217; Expressed in right lobe of liver and 118 other cell types or tissues. DR ExpressionAtlas; O75191; baseline and differential. 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; IDA:UniProtKB. DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc. DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc. DR GO; GO:0019640; P:glucuronate catabolic process to xylulose 5-phosphate; TAS:Reactome. DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central. DR GO; GO:0005998; P:xylulose catabolic process; TAS:BHF-UCL. DR GO; GO:0005997; P:xylulose metabolic process; IDA: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. DR Genevisible; O75191; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Carbohydrate metabolism; KW Kinase; Nucleotide-binding; Reference proteome; Transferase; KW Xylose metabolism. FT CHAIN 1..536 FT /note="Xylulose kinase" FT /id="PRO_0000230985" FT BINDING 99 FT /ligand="substrate" FT BINDING 170 FT /ligand="substrate" FT BINDING 280 FT /ligand="substrate" FT BINDING 281 FT /ligand="substrate" FT BINDING 355 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 441..442 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 445 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT VAR_SEQ 1..137 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055522" FT VARIANT 85 FT /note="D -> E (in dbSNP:rs17118)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:9763671, ECO:0000269|Ref.3" FT /id="VAR_055151" FT VARIANT 133 FT /note="D -> N (in dbSNP:rs2234610)" FT /id="VAR_055152" FT VARIANT 139 FT /note="D -> E (in dbSNP:rs151611)" FT /id="VAR_055153" FT VARIANT 262 FT /note="Y -> N (in dbSNP:rs196380)" FT /evidence="ECO:0000269|PubMed:9763671" FT /id="VAR_055154" FT VARIANT 348 FT /note="N -> D (in dbSNP:rs2234622)" FT /id="VAR_055155" FT STRAND 9..15 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 17..26 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 31..38 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 39..42 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 44..46 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 52..54 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 61..64 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 65..81 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 86..88 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 89..96 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 101..105 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 108..113 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 121..125 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 132..135 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 143..153 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 156..163 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 172..182 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 184..188 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 190..195 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 196..205 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 213..216 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 218..220 FT /evidence="ECO:0007829|PDB:4BC4" FT TURN 224..227 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 231..237 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 241..245 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 254..257 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 260..266 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 273..275 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 280..287 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 295..311 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 316..323 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 326..339 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 340..350 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 355..363 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 369..371 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 373..379 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 382..384 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 388..392 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 398..400 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 404..425 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 436..440 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 441..444 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 446..456 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 460..462 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 468..481 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 484..486 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 489..493 FT /evidence="ECO:0007829|PDB:4BC3" FT STRAND 500..503 FT /evidence="ECO:0007829|PDB:4BC3" FT HELIX 509..530 FT /evidence="ECO:0007829|PDB:4BC3" SQ SEQUENCE 536 AA; 58382 MW; E2FC1C45308D71A8 CRC64; MAEHAPRRCC LGWDFSTQQV KVVAVDAELN VFYEESVHFD RDLPEFGTQG GVHVHKDGLT VTSPVLMWVQ ALDIILEKMK ASGFDFSQVL ALSGAGQQHG SIYWKAGAQQ ALTSLSPDLR LHQQLQDCFS ISDCPVWMDS STTAQCRQLE AAVGGAQALS CLTGSRAYER FTGNQIAKIY QQNPEAYSHT ERISLVSSFA ASLFLGSYSP IDYSDGSGMN LLQIQDKVWS QACLGACAPH LEEKLSPPVP SCSVVGAISS YYVQRYGFPP GCKVVAFTGD NPASLAGMRL EEGDIAVSLG TSDTLFLWLQ EPMPALEGHI FCNPVDSQHY MALLCFKNGS LMREKIRNES VSRSWSDFSK ALQSTEMGNG GNLGFYFDVM EITPEIIGRH RFNTENHKVA AFPGDVEVRA LIEGQFMAKR IHAEGLGYRV MSKTKILATG GASHNREILQ VLADVFDAPV YVIDTANSAC VGSAYRAFHG LAGGTDVPFS EVVKLAPNPR LAATPSPGAS QVYEALLPQY AKLEQRILSQ TRGPPE //