XK2_ARATH
ID XK2_ARATH Reviewed; 558 AA.
AC Q949W8; Q9LT51;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Xylulose kinase 2 {ECO:0000303|PubMed:16920870};
DE Short=Atxk-2 {ECO:0000303|PubMed:16920870};
DE Short=Xylulokinase 2 {ECO:0000305};
DE EC=2.7.1.17 {ECO:0000269|PubMed:16920870};
DE AltName: Full=1-Deoxy-D-Xylulokinase {ECO:0000303|PubMed:16920870};
DE Short=DXK {ECO:0000303|PubMed:16920870};
GN Name=XK2 {ECO:0000303|PubMed:16920870};
GN Synonyms=XK-2 {ECO:0000303|PubMed:16920870};
GN OrderedLocusNames=At5g49650 {ECO:0000312|Araport:AT5G49650};
GN ORFNames=MNI5.3 {ECO:0000312|EMBL:BAA97229.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP IDENTIFICATION BY MASS SPECTROMETRY, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=16920870; DOI=10.1104/pp.106.086652;
RA Hemmerlin A., Tritsch D., Hartmann M., Pacaud K., Hoeffler J.F.,
RA van Dorsselaer A., Rohmer M., Bach T.J.;
RT "A cytosolic Arabidopsis D-xylulose kinase catalyzes the phosphorylation of
RT 1-deoxy-D-xylulose into a precursor of the plastidial isoprenoid pathway.";
RL Plant Physiol. 142:441-457(2006).
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:0000269|PubMed:16920870}.
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:16920870};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:P11553};
CC -!- ACTIVITY REGULATION: Repressed by oxo-clomazone (keto-clomazone), a
CC bleaching herbicide. {ECO:0000269|PubMed:16920870}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.07 mM for D-xylulose (at pH 8) {ECO:0000269|PubMed:16920870};
CC KM=4 mM for 1-deoxy-D-xylulose (at pH 8)
CC {ECO:0000269|PubMed:16920870};
CC Vmax=357 mmol/min/mg enzyme with D-xylulose (at pH 8)
CC {ECO:0000269|PubMed:16920870};
CC Vmax=120 mmol/min/mg enzyme with 1-deoxy-D-xylulose as substrate (at
CC pH 8) {ECO:0000269|PubMed:16920870};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius (at pH 8). Active from 10
CC to 50 degrees Celsius. {ECO:0000269|PubMed:16920870};
CC -!- PATHWAY: Isoprenoid biosynthesis; carotenoid biosynthesis.
CC {ECO:0000305|PubMed:16920870}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16920870}.
CC -!- DISRUPTION PHENOTYPE: Impaired xylulose kinase activity in cytoplasm.
CC Hypersensitivity to D-xylulose (Xyl) leading to reduced seeds
CC germination. Loss of remediation of photosynthetic pigments after oxo-
CC clomazone-mediated bleaching, thus leading to albino plants.
CC {ECO:0000269|PubMed:16920870}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97229.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB025627; BAA97229.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95841.1; -; Genomic_DNA.
DR EMBL; AY050843; AAK92778.1; -; mRNA.
DR EMBL; AY142596; AAN13165.1; -; mRNA.
DR RefSeq; NP_199776.1; NM_124343.2.
DR AlphaFoldDB; Q949W8; -.
DR SMR; Q949W8; -.
DR STRING; 3702.AT5G49650.1; -.
DR PaxDb; Q949W8; -.
DR PRIDE; Q949W8; -.
DR ProteomicsDB; 242467; -.
DR DNASU; 835027; -.
DR EnsemblPlants; AT5G49650.1; AT5G49650.1; AT5G49650.
DR GeneID; 835027; -.
DR Gramene; AT5G49650.1; AT5G49650.1; AT5G49650.
DR KEGG; ath:AT5G49650; -.
DR Araport; AT5G49650; -.
DR TAIR; locus:2168902; AT5G49650.
DR eggNOG; KOG2531; Eukaryota.
DR HOGENOM; CLU_016149_8_0_1; -.
DR InParanoid; Q949W8; -.
DR OMA; QHGTVFW; -.
DR OrthoDB; 592116at2759; -.
DR PhylomeDB; Q949W8; -.
DR BioCyc; ARA:AT5G49650-MON; -.
DR UniPathway; UPA00386; -.
DR PRO; PR:Q949W8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q949W8; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
DR GO; GO:0004856; F:xylulokinase activity; IDA:TAIR.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR GO; GO:0005997; P:xylulose metabolic process; IMP:TAIR.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..558
FT /note="Xylulose kinase 2"
FT /id="PRO_0000443300"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q31KC7"
FT BINDING 20..23
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q31KC7"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q31KC7"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q31KC7"
FT BINDING 305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8L794"
FT BINDING 456..460
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8L794"
SQ SEQUENCE 558 AA; 61295 MW; CCA2D5FE98ED24B3 CRC64;
MADLSLPPDS LFLGFDSSTQ SMKATVLDSN LNIIKTELVH FDSDLPQYKT KDGVYRDTTV
NGRIVSPTLM WVEAFDLILQ KLSNANFDFA KVIAVSGSGQ QHGSVYWSKG SSEVLRSLDS
KRSLKEQLEN AFSVKESPIW MDSSTTLQCK EIENAVGGAM ELSKITGSRA YERFTGPQIR
KLFMTQGEVY KSTERISLVS SFMASLLVGD YACIDETDAA GMNLMDIEKR CWSKAALEAT
ATGLEEKLGK LAPAYATAGS ISQYFVQRFG FEKNCVVVQW SGDNPNSLAG LTLSTPGDLA
ISLGTSDTVF GITKELQPSL EGHVLPNPVD PESYMVMLVY KNASLTREEI RDRCAEGSWD
VFNKYLQQTQ PLNNGKLGFY YTENEILPPL PVGSHRYILE NFSGESLEGV KEQEVGEFDP
PSEVRALIEG QFLSKRAHTE RFGMPSPPLR IIATGGASAN ENILSLISAI FGCDVYTVQR
PDSASLGAAL RAAHGWLCNK KGSFVPISNL YEGKLETTSL NCKLKVKAGD ANIASTYGLL
MKKRMEIENK LVEKLGHF
