UKL1_ARATH
ID UKL1_ARATH Reviewed; 486 AA.
AC Q9FKS0; Q8RXX1;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Uridine/cytidine kinase UKL1, chloroplastic {ECO:0000305};
DE EC=2.7.1.48 {ECO:0000269|PubMed:21828290, ECO:0000269|PubMed:31101721, ECO:0000269|PubMed:31907295};
DE AltName: Full=AtUK {ECO:0000305};
DE AltName: Full=Uridine kinase-like protein 1 {ECO:0000303|PubMed:19563437};
DE AltName: Full=Uridine/cytidine kinase 1 {ECO:0000303|PubMed:31101721};
DE Flags: Precursor;
GN Name=UKL1 {ECO:0000303|PubMed:19563437};
GN Synonyms=UCK1 {ECO:0000303|PubMed:31101721},
GN UK {ECO:0000303|PubMed:17143579}, UPRT1 {ECO:0000303|PubMed:17143579};
GN OrderedLocusNames=At5g40870 {ECO:0000312|Araport:AT5G40870};
GN ORFNames=MHK7.10 {ECO:0000312|EMBL:BAB11349.1};
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17143579; DOI=10.1007/s11103-006-9101-3;
RA Islam M.R., Kim H., Kang S.W., Kim J.S., Jeong Y.M., Hwang H.J., Lee S.Y.,
RA Woo J.C., Kim S.G.;
RT "Functional characterization of a gene encoding a dual domain for uridine
RT kinase and uracil phosphoribosyltransferase in Arabidopsis thaliana.";
RL Plant Mol. Biol. 63:465-477(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [3]
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 [4]
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19563437; DOI=10.1111/j.1365-313x.2009.03963.x;
RA Mainguet S.E., Gakiere B., Majira A., Pelletier S., Bringel F., Guerard F.,
RA Caboche M., Berthome R., Renou J.P.;
RT "Uracil salvage is necessary for early Arabidopsis development.";
RL Plant J. 60:280-291(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21828290; DOI=10.1105/tpc.111.085829;
RA Chen M., Thelen J.J.;
RT "Plastid uridine salvage activity is required for photoassimilate
RT allocation and partitioning in Arabidopsis.";
RL Plant Cell 23:2991-3006(2011).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=31101721; DOI=10.1104/pp.19.00329;
RA Ohler L., Niopek-Witz S., Mainguet S.E., Moehlmann T.;
RT "Pyrimidine salvage: physiological functions and interaction with
RT chloroplast biogenesis.";
RL Plant Physiol. 180:1816-1828(2019).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31907295; DOI=10.1105/tpc.19.00639;
RA Chen M., Witte C.P.;
RT "A kinase and a glycosylase catabolize pseudouridine in the peroxisome to
RT prevent toxic pseudouridine monophosphate accumulation.";
RL Plant Cell 32:722-739(2020).
CC -!- FUNCTION: Involved in the pyrimidine salvage pathway (Probable)
CC (PubMed:21828290, PubMed:31101721, PubMed:31907295). Phosphorylates
CC uridine to uridine monophosphate (UMP) (PubMed:21828290,
CC PubMed:31101721, PubMed:31907295). Phosphorylates cytidine to cytidine
CC monophosphate (CMP) (PubMed:31101721). Does not possess uracil
CC phosphoribosyltransferase (UPRTase) activity that catalyzes the
CC conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP)
CC to UMP and diphosphate (PubMed:19563437, PubMed:21828290,
CC PubMed:31101721). {ECO:0000269|PubMed:19563437,
CC ECO:0000269|PubMed:21828290, ECO:0000269|PubMed:31101721,
CC ECO:0000269|PubMed:31907295, ECO:0000305|PubMed:17143579}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cytidine = ADP + CMP + H(+); Xref=Rhea:RHEA:24674,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17562, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC Evidence={ECO:0000269|PubMed:31101721};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24675;
CC Evidence={ECO:0000269|PubMed:31101721};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + uridine = ADP + H(+) + UMP; Xref=Rhea:RHEA:16825,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC Evidence={ECO:0000269|PubMed:21828290, ECO:0000269|PubMed:31101721,
CC ECO:0000269|PubMed:31907295};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16826;
CC Evidence={ECO:0000269|PubMed:21828290, ECO:0000269|PubMed:31101721,
CC ECO:0000269|PubMed:31907295};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.33 uM for cytidine {ECO:0000269|PubMed:31101721};
CC KM=0.34 uM for uridine {ECO:0000269|PubMed:21828290};
CC Vmax=4.66 umol/h/mg enzyme with cytidine as substrate
CC {ECO:0000269|PubMed:31101721};
CC Vmax=14.8 umol/h/mg enzyme with uridine as substrate
CC {ECO:0000269|PubMed:21828290};
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC CTP from cytidine: step 1/3. {ECO:0000305}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uridine: step 1/1. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:21828290}. Cytoplasm {ECO:0000269|PubMed:17143579}.
CC Note=Aggregates in granular precipitates restricted to the cytoplasm,
CC when expressed in transfected cells. {ECO:0000269|PubMed:17143579}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and stems.
CC {ECO:0000269|PubMed:17143579}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:17143579, PubMed:19563437). No decrease in uracil
CC phosphoribosyltransferase activity (PubMed:17143579, PubMed:19563437).
CC Loss of sensitivity to 5'-fluorouracil and 5'-fluorouridine
CC (PubMed:17143579, PubMed:21828290). {ECO:0000269|PubMed:17143579,
CC ECO:0000269|PubMed:19563437, ECO:0000269|PubMed:21828290}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the uridine kinase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the UPRTase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was prevsiouly characterized as an enzyme that possesses
CC uracil phosphoribosyltransferase (UPRT) activity (PubMed:17143579).
CC Further publications show a lack of such activity (PubMed:19563437,
CC PubMed:21828290). {ECO:0000269|PubMed:17143579,
CC ECO:0000269|PubMed:19563437, ECO:0000269|PubMed:21828290}.
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DR EMBL; AB011477; BAB11349.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94610.1; -; Genomic_DNA.
DR EMBL; AY080631; AAL85977.1; -; mRNA.
DR EMBL; AY089970; AAM10488.1; -; mRNA.
DR EMBL; BT002336; AAN86169.1; -; mRNA.
DR RefSeq; NP_198903.1; NM_123452.5.
DR AlphaFoldDB; Q9FKS0; -.
DR SMR; Q9FKS0; -.
DR BioGRID; 19339; 3.
DR STRING; 3702.AT5G40870.1; -.
DR iPTMnet; Q9FKS0; -.
DR PaxDb; Q9FKS0; -.
DR PRIDE; Q9FKS0; -.
DR ProteomicsDB; 245303; -.
DR EnsemblPlants; AT5G40870.1; AT5G40870.1; AT5G40870.
DR GeneID; 834088; -.
DR Gramene; AT5G40870.1; AT5G40870.1; AT5G40870.
DR KEGG; ath:AT5G40870; -.
DR Araport; AT5G40870; -.
DR TAIR; locus:2164516; AT5G40870.
DR eggNOG; KOG4203; Eukaryota.
DR HOGENOM; CLU_021278_0_3_1; -.
DR InParanoid; Q9FKS0; -.
DR OMA; RTKTMYG; -.
DR OrthoDB; 929897at2759; -.
DR PhylomeDB; Q9FKS0; -.
DR BioCyc; ARA:AT5G40870-MON; -.
DR BRENDA; 2.4.2.9; 399.
DR BRENDA; 2.7.1.48; 399.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR PRO; PR:Q9FKS0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKS0; baseline and differential.
DR Genevisible; Q9FKS0; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004849; F:uridine kinase activity; IDA:TAIR.
DR GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:2000904; P:regulation of starch metabolic process; IMP:TAIR.
DR GO; GO:0044206; P:UMP salvage; IDA:TAIR.
DR CDD; cd06223; PRTases_typeI; 1.
DR CDD; cd02023; UMPK; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR006083; PRK/URK.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR029930; UCKL1_plant.
DR InterPro; IPR000764; Uridine_kinase-like.
DR PANTHER; PTHR10285:SF142; PTHR10285:SF142; 1.
DR Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR00235; udk; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Chloroplast; Cytoplasm; Glycosyltransferase;
KW GTP-binding; Kinase; Multifunctional enzyme; Nucleotide-binding; Plastid;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..486
FT /note="Uridine/cytidine kinase UKL1, chloroplastic"
FT /id="PRO_0000394514"
FT REGION 31..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..264
FT /note="Uridine kinase"
FT REGION 274..486
FT /note="Uracil phosphoribosyltransferase"
FT COMPBIAS 31..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 298
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 341..344
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 407..410
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 472..474
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250"
FT BINDING 473
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
SQ SEQUENCE 486 AA; 54430 MW; 50DA1CE89346FB54 CRC64;
MPEDSSSLDY AMEKASGPHF SGLRFDGLLS SSPPNSSVVS SLRSAVSSSS PSSSDPEAPK
QPFIIGVSGG TASGKTTVCD MIIQQLHDHR VVLVNQDSFY RGLTSEELQR VQEYNFDHPD
AFDTEQLLHC AETLKSGQPY QVPIYDFKTH QRRSDTFRQV NASDVIILEG ILVFHDSRVR
NLMNMKIFVD TDADVRLARR IRRDTVERGR DVNSVLEQYA KFVKPAFDDF VLPSKKYADV
IIPRGGDNHV AVDLITQHIH TKLGQHDLCK IYPNVYVIQS TFQIRGMHTL IREKDISKHD
FVFYSDRLIR LVVEHGLGHL PFTEKQVVTP TGAVYTGVDF CKKLCGVSII RSGESMENAL
RACCKGIKIG KILIHRDGDN GKQLIYEKLP HDISERHVLL LDPVLATGNS ANQAIELLIQ
KGVPEAHIIF LNLISAPEGI HCVCKRFPAL KIVTSEIDQC LNQEFRVIPG LGEFGDRYFG
TDEEDQ
