ID XYLB_PONAB Reviewed; 580 AA. AC Q5R830; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 24-JAN-2024, entry version 62. DE RecName: Full=Xylulose kinase; DE Short=Xylulokinase; DE EC=2.7.1.17; GN Name=XYLB; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pongo. OX NCBI_TaxID=9601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. 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 --------------------------------------------------------------------------- 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; CR859925; CAH92080.1; -; mRNA. DR RefSeq; NP_001126213.1; NM_001132741.1. DR AlphaFoldDB; Q5R830; -. DR SMR; Q5R830; -. DR STRING; 9601.ENSPPYP00000015667; -. DR GeneID; 100173181; -. DR KEGG; pon:100173181; -. DR CTD; 9942; -. DR eggNOG; KOG2531; Eukaryota. DR InParanoid; Q5R830; -. DR OrthoDB; 1704034at2759; -. DR Proteomes; UP000001595; Unplaced. 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: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 2: Evidence at transcript level; KW ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding; KW Reference proteome; Transferase; Xylose metabolism. FT CHAIN 1..580 FT /note="Xylulose kinase" FT /id="PRO_0000230987" FT BINDING 99 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 170 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 280 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 281 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 355 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 441..442 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 445 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" SQ SEQUENCE 580 AA; 62905 MW; BAE8DFB1EDF9FF0C CRC64; MAEHAPRRCC LGWDFSTQQV KVVAVDAELN VFYEESVHFD RDLPEFGTQG GVHVHKDGLT VTSPVLMWVQ ALDIILEKMK ASGFDFSQVL ALSGAGQQHG SIYWKAGSQQ ALTSLSPDLP LHQQLQDCFS ISDCPVWMDS SSTTQCRQLE AAMGGAQALS CLTGSRAYER FTGNQIAKIY QQNPEAYSHT ERISLVSSFA ASLFLGSYSP IDYSDGSGMN LLQIQDKVWS QACLGACAPH LEEKLGPPVP SCSVVGAISS YYVQRYGFPP GCKVVAFTGD NPASLAGMRL EEGDIAVSLG TSDTLFLWLQ EPMPALEGHI FCNPVDSQHY MALLCFKNGS LMREKIRDES ASRSWSDFSK ALQSTEMGNG GNLGFYFDVM EITPEIIGRH RFNTENHKVA AFPGDVEVRA LIEGQFMAKR IHAEGLGYRV MSKTKILATG GASHNRDILQ VLADVFGAPV YVIDTANSAC VGSAYRAFHG LAGGTDVPFS EVVKLAPNPR LAATPSPGAS QRRWVGVSTT KLVSASDAQH RGSNLGRRVA GAMVRKCGTM LEDTRVLLKQ SSWPKPAANL DIIKTPETLS //