XYLB_PONAB
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 03-AUG-2022, entry version 59.
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}.
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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; 592116at2759; -.
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 InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
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 PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; SSF53067; 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