UKL5_ARATH
ID UKL5_ARATH Reviewed; 465 AA.
AC Q9LTY6;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Uridine kinase-like protein 5;
DE Includes:
DE RecName: Full=Probable uridine kinase;
DE Short=UK;
DE EC=2.7.1.48;
DE Includes:
DE RecName: Full=Probable uracil phosphoribosyltransferase;
DE Short=UPRTase;
DE EC=2.4.2.9;
DE AltName: Full=UMP pyrophosphorylase;
GN Name=UKL5; OrderedLocusNames=At3g27440; ORFNames=K1G2.27;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 FUNCTION, 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).
CC -!- FUNCTION: Involved in the pyrimidine salvage pathway. {ECO:0000250,
CC ECO:0000269|PubMed:19563437}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC uracil; Xref=Rhea:RHEA:13017, ChEBI:CHEBI:17568, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:58017; EC=2.4.2.9;
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
CC {ECO:0000250};
CC -!- ACTIVITY REGULATION: Allosterically activated by GTP. {ECO:0000250}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uracil: step 1/1.
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC CTP from cytidine: step 1/3.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uridine: step 1/1.
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}.
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DR EMBL; AB024028; BAA95720.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77321.1; -; Genomic_DNA.
DR RefSeq; NP_189380.1; NM_113659.2.
DR AlphaFoldDB; Q9LTY6; -.
DR SMR; Q9LTY6; -.
DR BioGRID; 7695; 1.
DR STRING; 3702.AT3G27440.1; -.
DR PaxDb; Q9LTY6; -.
DR PRIDE; Q9LTY6; -.
DR ProteomicsDB; 246397; -.
DR EnsemblPlants; AT3G27440.1; AT3G27440.1; AT3G27440.
DR GeneID; 822365; -.
DR Gramene; AT3G27440.1; AT3G27440.1; AT3G27440.
DR KEGG; ath:AT3G27440; -.
DR Araport; AT3G27440; -.
DR TAIR; locus:2086691; AT3G27440.
DR eggNOG; KOG4203; Eukaryota.
DR HOGENOM; CLU_021278_3_0_1; -.
DR InParanoid; Q9LTY6; -.
DR OMA; HQSIEPA; -.
DR OrthoDB; 929897at2759; -.
DR PhylomeDB; Q9LTY6; -.
DR BioCyc; ARA:AT3G27440-MON; -.
DR UniPathway; UPA00574; UER00636.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR PRO; PR:Q9LTY6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LTY6; baseline and differential.
DR Genevisible; Q9LTY6; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004849; F:uridine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
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; IPR000764; Uridine_kinase-like.
DR Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR00235; udk; 1.
PE 2: Evidence at transcript level;
KW Allosteric enzyme; Glycosyltransferase; GTP-binding; Kinase;
KW Multifunctional enzyme; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..465
FT /note="Uridine kinase-like protein 5"
FT /id="PRO_0000394517"
FT REGION 26..230
FT /note="Uridine kinase"
FT /evidence="ECO:0000250"
FT REGION 240..465
FT /note="Uracil phosphoribosyltransferase"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 307..310
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 373..376
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 438..440
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
SQ SEQUENCE 465 AA; 52125 MW; 4CD82DB9059E7168 CRC64;
MEKLSNGVRD HCLISDYVSP SAPAPLKQPF VIGVAGGTAS GKTTVCNMIM SQLHDQRVVL
VNQDSFYHSL TKEKLNKVHE YNFDHPDAFN TEVLLSCMEK LRSGQPVNIP SYDFKIHQSI
ESSSPVNPGD VIILEGILVL NDPRVRDLMN MKIFVDTDAD VRLSRRIQRD TVERGRNIQN
VLEQYTKFVK PSFDEYIQPS MKYADIIIPR GGDNDVAIDL IVQHIRTKLC QHNLCKIYSN
IFIISSTFQI KGMHTLIRDI NTTKHDFVFY ADRLIRLVVE HGLGHLPFTE KQITTPTGSV
YTGVDFCKRL CGVSVIRSGE SMENALRACC NGIKIGKILI HRENNDGRQL IYEKLPKDIS
SRHVFLLDPV LASGYSAVKA ITLLLSKGVP ESHIIFLNLI AAPQGIHALC KKFPMLKIVT
SEIDSSLNED SRVIPGLGEF ADRYFGTNNI NSKVSSLSTN LKLRS
