XK1_ARATH
ID XK1_ARATH Reviewed; 478 AA.
AC Q8L794; Q67XN5; Q9SJU1;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=D-ribulose kinase {ECO:0000305|PubMed:27223615};
DE Short=D-ribulokinase {ECO:0000305};
DE EC=2.7.1.47 {ECO:0000269|PubMed:27223615};
DE AltName: Full=Inactive Xylulose kinase 1 {ECO:0000303|PubMed:16920870};
DE Short=Atxk-1 {ECO:0000303|PubMed:16920870};
DE Flags: Precursor;
GN Name=XK1 {ECO:0000303|PubMed:16920870};
GN Synonyms=XK-1 {ECO:0000303|PubMed:16920870};
GN OrderedLocusNames=At2g21370 {ECO:0000312|Araport:AT2G21370};
GN ORFNames=F3K23.13 {ECO:0000312|EMBL:AAD23698.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION.
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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 43-478 IN COMPLEX WITH ADP AND
RP ATP ANALOG, AND FUNCTION.
RX PubMed=27223615; DOI=10.1371/journal.pone.0156067;
RA Xie Y., Li M., Chang W.;
RT "Crystal structures of putative sugar kinases from Synechococcus elongatus
RT PCC 7942 and Arabidopsis thaliana.";
RL PLoS ONE 11:E0156067-E0156067(2016).
CC -!- FUNCTION: Exhibits ATP hydrolysis without substrate. Can phosphorylate
CC D-ribulose with low efficiency. {ECO:0000269|PubMed:27223615}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+);
CC Xref=Rhea:RHEA:17601, ChEBI:CHEBI:15378, ChEBI:CHEBI:17173,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58121, ChEBI:CHEBI:456216;
CC EC=2.7.1.47; Evidence={ECO:0000269|PubMed:27223615};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:P11553};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16920870}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8L794-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8L794-2; Sequence=VSP_059328;
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD23698.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006841; AAD23698.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07166.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07167.1; -; Genomic_DNA.
DR EMBL; AY136397; AAM97063.1; -; mRNA.
DR EMBL; BT000210; AAN15529.1; -; mRNA.
DR EMBL; AK175657; BAD43420.1; -; mRNA.
DR EMBL; AK176783; BAD44546.1; -; mRNA.
DR PIR; D84600; D84600.
DR RefSeq; NP_179732.2; NM_127708.3. [Q8L794-1]
DR RefSeq; NP_973505.1; NM_201776.3. [Q8L794-2]
DR PDB; 5HTR; X-ray; 2.00 A; A=43-478.
DR PDB; 5HTV; X-ray; 1.78 A; A=43-478.
DR PDB; 5HTX; X-ray; 1.49 A; A=43-478.
DR PDBsum; 5HTR; -.
DR PDBsum; 5HTV; -.
DR PDBsum; 5HTX; -.
DR AlphaFoldDB; Q8L794; -.
DR SMR; Q8L794; -.
DR STRING; 3702.AT2G21370.1; -.
DR iPTMnet; Q8L794; -.
DR PaxDb; Q8L794; -.
DR PRIDE; Q8L794; -.
DR ProteomicsDB; 242525; -. [Q8L794-1]
DR EnsemblPlants; AT2G21370.1; AT2G21370.1; AT2G21370. [Q8L794-1]
DR EnsemblPlants; AT2G21370.2; AT2G21370.2; AT2G21370. [Q8L794-2]
DR GeneID; 816675; -.
DR Gramene; AT2G21370.1; AT2G21370.1; AT2G21370. [Q8L794-1]
DR Gramene; AT2G21370.2; AT2G21370.2; AT2G21370. [Q8L794-2]
DR KEGG; ath:AT2G21370; -.
DR Araport; AT2G21370; -.
DR TAIR; locus:2050029; AT2G21370.
DR eggNOG; ENOG502QVMB; Eukaryota.
DR InParanoid; Q8L794; -.
DR OMA; FLHQADW; -.
DR OrthoDB; 1252682at2759; -.
DR PhylomeDB; Q8L794; -.
DR PRO; PR:Q8L794; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8L794; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0019150; F:D-ribulokinase activity; IDA:UniProtKB.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Chloroplast; Kinase;
KW Nucleotide-binding; Plastid; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..38
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 39..478
FT /note="D-ribulose kinase"
FT /id="PRO_0000443299"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q31KC7"
FT BINDING 64..67
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q31KC7"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q31KC7"
FT BINDING 300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27223615,
FT ECO:0007744|PDB:5HTV, ECO:0007744|PDB:5HTX"
FT BINDING 338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27223615,
FT ECO:0007744|PDB:5HTV, ECO:0007744|PDB:5HTX"
FT BINDING 433..437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27223615,
FT ECO:0007744|PDB:5HTV, ECO:0007744|PDB:5HTX"
FT VAR_SEQ 1..93
FT /note="Missing (in isoform 2)"
FT /id="VSP_059328"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:5HTX"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:5HTX"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:5HTX"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:5HTX"
FT HELIX 96..110
FT /evidence="ECO:0007829|PDB:5HTX"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:5HTX"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:5HTX"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:5HTX"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:5HTX"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:5HTX"
FT HELIX 156..162
FT /evidence="ECO:0007829|PDB:5HTX"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:5HTX"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:5HTX"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:5HTX"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:5HTX"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:5HTX"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:5HTX"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:5HTX"
FT TURN 225..228
FT /evidence="ECO:0007829|PDB:5HTX"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:5HTX"
FT HELIX 238..242
FT /evidence="ECO:0007829|PDB:5HTX"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:5HTX"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:5HTX"
FT HELIX 258..264
FT /evidence="ECO:0007829|PDB:5HTX"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:5HTX"
FT HELIX 278..285
FT /evidence="ECO:0007829|PDB:5HTX"
FT STRAND 293..310
FT /evidence="ECO:0007829|PDB:5HTX"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:5HTX"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:5HTX"
FT STRAND 327..335
FT /evidence="ECO:0007829|PDB:5HTX"
FT HELIX 338..344
FT /evidence="ECO:0007829|PDB:5HTX"
FT HELIX 347..355
FT /evidence="ECO:0007829|PDB:5HTX"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:5HTX"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:5HTX"
FT HELIX 395..419
FT /evidence="ECO:0007829|PDB:5HTX"
FT STRAND 427..432
FT /evidence="ECO:0007829|PDB:5HTX"
FT HELIX 433..436
FT /evidence="ECO:0007829|PDB:5HTX"
FT HELIX 438..448
FT /evidence="ECO:0007829|PDB:5HTX"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:5HTX"
FT HELIX 460..475
FT /evidence="ECO:0007829|PDB:5HTX"
SQ SEQUENCE 478 AA; 52468 MW; B1BBCA3FCD107D3F CRC64;
MLILRQFQIS SFELFQSPKQ TGFYSSSRSV PLPRTRFYSD FRVMSGNKGT NYEKLYLGMD
FGTSGGRFTV IDEQGEIKAQ GKREYPPFMK EESMGWASSW KATLFSLLED IPVTVRSLVS
SISLDGTSAT TLILNSESGE VLCQPYLYNQ SCPDALPEVK SIAPANHTVC SGTSTLCKLV
SWWNTEVPNR ESAVLLHQAD WLLWLLHGRL GVSDYNNALK VGYDPESESY PSWLLGQPYS
QLLPKVQAPG TSIGNLKESF TRQFGFPDDC IVCTGTTDSI AAFLAARATE PGKAVTSLGS
TLAIKLLSTK RVDDARYGVY SHRLDDKWLV GGASNTGGAI LRQLFSDEQL ERLSQEINPM
VGSPLDYYPL QSSGERFPIA DPNLAPRLLP RPESDVEFLH GILESIARIE GKGYKLLKEL
GATEAEEVLT AGGGAKNDKW IKIRQRVLGL PVKKAVHTEA SYGASLLALK GAKQNSGL
