ID D7MPD2_ARALL Unreviewed; 564 AA.
AC D7MPD2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Xylulose kinase {ECO:0000256|RuleBase:RU367058};
DE EC=2.7.1.17 {ECO:0000256|RuleBase:RU367058};
GN ORFNames=ARALYDRAFT_495023 {ECO:0000313|EMBL:EFH40263.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- FUNCTION: Mediates 1-deoxy-D-xylulose (DX) phosphorylation in the
CC cytoplasm prior to the translocation of 1-deoxy-D-xylulose 5-phosphate
CC into plastids. Can also phosphorylate D-xylulose (Xyl). Uses
CC preferentially ATP as cosubstrate. {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; GL348720; EFH40263.1; -; Genomic_DNA.
DR RefSeq; XP_002864004.1; XM_002863958.1.
DR AlphaFoldDB; D7MPD2; -.
DR STRING; 81972.D7MPD2; -.
DR EnsemblPlants; fgenesh2_kg.8__839__AT5G49650.1; fgenesh2_kg.8__839__AT5G49650.1; fgenesh2_kg.8__839__AT5G49650.1.
DR Gramene; fgenesh2_kg.8__839__AT5G49650.1; fgenesh2_kg.8__839__AT5G49650.1; fgenesh2_kg.8__839__AT5G49650.1.
DR eggNOG; KOG2531; Eukaryota.
DR HOGENOM; CLU_016149_8_0_1; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblPlants.
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:EnsemblPlants.
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, ECO:0000313|EMBL:EFH40263.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367058};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Transferase {ECO:0000256|RuleBase:RU367058};
KW Xylose metabolism {ECO:0000256|RuleBase:RU367058}.
FT DOMAIN 12..288
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 299..502
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 564 AA; 61923 MW; 931963D998FACB91 CRC64;
MADLSLPPDS IFLGFDSSTQ SLKATVLDSN LNIVKTELVH FDSDLPHYKT KDGVYRDTTV
NGRIVSPTLM WVEAFDLILQ KLSNANFDFG KVIAVSGSGQ QHGSVYWSKG SSEVLKSLDS
KRCLKDQLEN AFSVKESPIW MDSSTTLQCK EIENAVGGAM ELSQITGSRA YERFTGPQIR
KLFTTQGDTY KSTERISLVS SFMASLLIGD YASIDETDAA GMNLMDIKKR CWSKAALEAT
ATGLEEKLGK LAPAYATAGS ISQYFVQRFG FEKNCVVVQW SGDNPNSLAG LTLSTPGDLA
ISLGTSDTAR LLILVFGITK ELQPSLEGHV LPNPVDPESY MVMLVYKNAS LTREEIRDRC
AEGSWDVFNK YLQQTQPLNN GKLGFYYTEN EILPPLPVGS HRYILENFSG ESLEGVKERE
ANEFDPPSEV RALIEGQFLS KRAHTERFGM PSPPIRIIAT GGASANENIL SLISAIFGCD
VYTVQRPDSA SLGAALRAAH GWLCNKKGSF VPISNLYEGK LETTSLNCKL KVKAGDANIA
STYGLLMKKR MEIENKLVEK LGHF
//
