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Database: UniProt/SWISS-PROT
Entry: UKL1_ARATH
LinkDB: UKL1_ARATH
Original site: 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   19-MAR-2014, entry version 93.
DE   RecName: Full=Uridine kinase-like protein 1, chloroplastic;
DE   Includes:
DE     RecName: Full=Uridine kinase;
DE              Short=UK;
DE              EC=2.7.1.48;
DE   Includes:
DE     RecName: Full=Putative uracil phosphoribosyltransferase;
DE              Short=UPRTase;
DE              EC=2.4.2.9;
DE     AltName: Full=UMP pyrophosphorylase;
DE   Flags: Precursor;
GN   Name=UKL1; Synonyms=UK/UPRT1; OrderedLocusNames=At5g40870;
GN   ORFNames=MHK7.10;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Lee S.Y., Woo J.C., Kim S.G.;
RT   "Functional characterization of a gene encoding a dual domain for
RT   uridine kinase and uracil phosphoribosyltransferase in Arabidopsis
RT   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
RT   physically assigned P1 and TAC clones.";
RL   DNA Res. 5:131-145(1998).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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.,
RA   Guerard F., 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).
CC   -!- FUNCTION: Involved in the pyrimidine salvage pathway. The uracil
CC       phosphoribosyltransferase (UPRT) activity, that catalyzes the
CC       conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate
CC       (PRPP) to UMP and diphosphate, is unsure.
CC   -!- CATALYTIC ACTIVITY: UMP + diphosphate = uracil + 5-phospho-alpha-
CC       D-ribose 1-diphosphate.
CC   -!- CATALYTIC ACTIVITY: ATP + cytidine = ADP + CMP.
CC   -!- CATALYTIC ACTIVITY: ATP + uridine = ADP + UMP.
CC   -!- COFACTOR: Binds 1 Mg(2+) ion per subunit. The magnesium is bound
CC       as Mg-PRPP (By similarity).
CC   -!- ENZYME REGULATION: Allosterically activated by GTP (By
CC       similarity).
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage
CC       pathway; UMP from uracil: step 1/1.
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage
CC       pathway; CTP from cytidine: step 1/3.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage
CC       pathway; UMP from uridine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast (Potential). Cytoplasm.
CC       Note=Aggregates in granular precipitates restricted to the
CC       cytoplasm, when expressed in transfected cells.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, roots, stems and flowers.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. No decrease in uracil
CC       phosphoribosyltransferase activity. Loss of sensitivity to 5'-
CC       fluorouracil and 5'-fluorouridine.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the uridine
CC       kinase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the UPRTase
CC       family.
CC   -!- CAUTION: Experiments shown in PubMed:17143579 indicate an uracil
CC       phosphoribosyltransferase (UPRT) activity, while PubMed:19563437
CC       shows a lack of such activity.
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DR   EMBL; AY089970; AAM10488.1; -; mRNA.
DR   EMBL; AB011477; BAB11349.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94610.1; -; Genomic_DNA.
DR   EMBL; AY080631; AAL85977.1; -; mRNA.
DR   EMBL; BT002336; AAN86169.1; -; mRNA.
DR   RefSeq; NP_198903.1; NM_123452.4.
DR   UniGene; At.9230; -.
DR   ProteinModelPortal; Q9FKS0; -.
DR   SMR; Q9FKS0; 61-263, 266-481.
DR   BioGrid; 19339; 1.
DR   STRING; 3702.AT5G40870.1-P; -.
DR   PaxDb; Q9FKS0; -.
DR   PRIDE; Q9FKS0; -.
DR   EnsemblPlants; AT5G40870.1; AT5G40870.1; AT5G40870.
DR   GeneID; 834088; -.
DR   KEGG; ath:AT5G40870; -.
DR   TAIR; AT5G40870; -.
DR   eggNOG; COG0572; -.
DR   HOGENOM; HOG000262757; -.
DR   InParanoid; Q9FKS0; -.
DR   KO; K00876; -.
DR   OMA; HVILMDS; -.
DR   PhylomeDB; Q9FKS0; -.
DR   ProtClustDB; CLSN2682673; -.
DR   BioCyc; ARA:AT5G40870-MONOMER; -.
DR   BRENDA; 2.4.2.9; 399.
DR   UniPathway; UPA00574; UER00636.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
DR   Genevestigator; Q9FKS0; -.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR   GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IGI:TAIR.
DR   GO; GO:0004849; F:uridine kinase activity; IDA:TAIR.
DR   GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:2000904; P:regulation of starch metabolic process; IMP:TAIR.
DR   GO; GO:0044206; P:UMP salvage; IDA:TAIR.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006083; PRK/URK.
DR   InterPro; IPR000764; Uridine_kinase.
DR   InterPro; IPR026008; Uridine_kinase-like.
DR   PANTHER; PTHR10285:SF6; PTHR10285:SF6; 1.
DR   Pfam; PF00485; PRK; 1.
DR   PRINTS; PR00988; URIDINKINASE.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00235; udk; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; Chloroplast; Complete proteome; Cytoplasm;
KW   Glycosyltransferase; GTP-binding; Kinase; Multifunctional enzyme;
KW   Nucleotide-binding; Plastid; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT       1     47       Chloroplast (Potential).
FT   CHAIN        48    486       Uridine kinase-like protein 1,
FT                                chloroplastic.
FT                                /FTId=PRO_0000394514.
FT   NP_BIND     341    344       GTP (By similarity).
FT   REGION       59    264       Uridine kinase.
FT   REGION      274    486       Uracil phosphoribosyltransferase.
FT   REGION      407    410       5-phospho-alpha-D-ribose 1-diphosphate
FT                                binding (By similarity).
FT   REGION      472    474       Uracil binding (By similarity).
FT   COMPBIAS     47     54       Poly-Ser.
FT   BINDING     298    298       GTP (By similarity).
FT   BINDING     307    307       GTP (By similarity).
FT   BINDING     351    351       5-phospho-alpha-D-ribose 1-diphosphate
FT                                (By similarity).
FT   BINDING     376    376       5-phospho-alpha-D-ribose 1-diphosphate
FT                                (By similarity).
FT   BINDING     396    396       GTP (By similarity).
FT   BINDING     402    402       5-phospho-alpha-D-ribose 1-diphosphate
FT                                (By similarity).
FT   BINDING     473    473       5-phospho-alpha-D-ribose 1-diphosphate
FT                                (By similarity).
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
//
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