ID A0A0M4EFW6_DROBS Unreviewed; 554 AA.
AC A0A0M4EFW6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Xylulose kinase {ECO:0000256|RuleBase:RU367058};
DE EC=2.7.1.17 {ECO:0000256|RuleBase:RU367058};
GN ORFNames=Dbus_chr3Rg1891 {ECO:0000313|EMBL:ALC47141.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC47141.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC47141.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC47141.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-2015) 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:0000256|RuleBase:RU367058}.
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:0000256|RuleBase:RU367058};
CC -!- SIMILARITY: Belongs to the FGGY kinase family.
CC {ECO:0000256|ARBA:ARBA00009156, ECO:0000256|RuleBase:RU367058}.
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DR EMBL; CP012526; ALC47141.1; -; Genomic_DNA.
DR RefSeq; XP_017849206.1; XM_017993717.1.
DR AlphaFoldDB; A0A0M4EFW6; -.
DR STRING; 30019.A0A0M4EFW6; -.
DR GeneID; 108604300; -.
DR OMA; STHFFNH; -.
DR OrthoDB; 1704034at2759; -.
DR Proteomes; UP000494163; Chromosome 3r sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004856; F:xylulokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0005997; P:xylulose metabolic process; IEA:UniProtKB-UniRule.
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; 2.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU367058};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU367058};
KW Kinase {ECO:0000256|RuleBase:RU367058};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367058};
KW Reference proteome {ECO:0000313|Proteomes:UP000494163};
KW Transferase {ECO:0000256|RuleBase:RU367058};
KW Xylose metabolism {ECO:0000256|RuleBase:RU367058}.
FT DOMAIN 128..290
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 299..493
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 554 AA; 61600 MW; 0437938F650DEB84 CRC64;
MPQQEEKPKR TFLGFDLSTQ KLKAILLNAE LNVVTTAEVK FDSDLPEFRT QGGANPGPNK
HEYFVQPVMW VKAMDIVLDR LVMQEADLST VVAISGSAQQ HGSLYWSKHG IASLNNLDAD
RFLHTQVDDS AFVLNRTPIW MDASTAKQCF EMETAIGGQT EMVQQTGSKC YARFTGPQIR
KIYQQRTHAY EDAQRISLVS SFLASIFLGK VAAIDYADGS GMNLLDIRNK TWSKACLNAC
APDLEERLGE TVSGLTVLGN ICDYFVQRFC FPPDCKVVAC TGDNPSALAG MLVDNNWLSI
SLGTSDTLMM CLEEPPNLEE GHVLCHPTET QQYMGLLCFR NGSLVREAIN KSEAGGNWDK
FNELLESTPR GNFGNMALHF NEVEIIPKAK GTLRWNKEVQ ASSHDAIKGI IKFSSPQIEI
RALIEGQMLH HRAISEDMGF HFGNETKILA TGGASVNKSI LQIIADVFNA PVYIQTESEA
ALLGAAYRAA YAYYINNNEH AESQPKGYRD YILSLTPNHL KLVCEPNKDS EAIYAPMLQR
YRDMALILEN NKSQ
//
