(data stored in SCRATCH zone)

SWISSPROT: UKL4_ARATH

ID   UKL4_ARATH              Reviewed;         469 AA.
AC   O65583; Q0WQS9; Q8LD95; Q9SYU2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   11-DEC-2019, entry version 131.
DE   RecName: Full=Uridine kinase-like protein 4;
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;
GN   Name=UKL4; Synonyms=UPT1; OrderedLocusNames=At4g26510; ORFNames=M3E9.60;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 297-469.
RC   STRAIN=cv. Columbia;
RA   Weers B.D., Thornburg R.W.;
RT   "Characterization of the cDNA and gene for an Arabidopsis thaliana uracil
RT   phosphoribosyltransferase.";
RL   (er) Plant Gene Register PGR99-044(1999).
RN   [7]
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. The uracil
CC       phosphoribosyltransferase (UPRT) activity, that catalyzes the
CC       conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP)
CC       to UMP and diphosphate, is unsure. {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA18219.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79506.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AL022223; CAA18219.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161565; CAB79506.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85211.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85212.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM66905.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM66906.1; -; Genomic_DNA.
DR   EMBL; AY086133; AAM63338.1; -; mRNA.
DR   EMBL; BT022059; AAY25471.1; -; mRNA.
DR   EMBL; AK228608; BAF00520.1; -; mRNA.
DR   EMBL; AF116860; AAD28199.1; -; mRNA.
DR   PIR; T05053; T05053.
DR   RefSeq; NP_001320072.1; NM_001341804.1.
DR   RefSeq; NP_001328772.1; NM_001341805.1.
DR   RefSeq; NP_567747.4; NM_118784.6.
DR   RefSeq; NP_849448.4; NM_179117.5.
DR   SMR; O65583; -.
DR   STRING; 3702.AT4G26510.1; -.
DR   iPTMnet; O65583; -.
DR   PaxDb; O65583; -.
DR   PRIDE; O65583; -.
DR   EnsemblPlants; AT4G26510.1; AT4G26510.1; AT4G26510.
DR   EnsemblPlants; AT4G26510.2; AT4G26510.2; AT4G26510.
DR   EnsemblPlants; AT4G26510.3; AT4G26510.3; AT4G26510.
DR   EnsemblPlants; AT4G26510.4; AT4G26510.4; AT4G26510.
DR   GeneID; 828757; -.
DR   Gramene; AT4G26510.1; AT4G26510.1; AT4G26510.
DR   Gramene; AT4G26510.2; AT4G26510.2; AT4G26510.
DR   Gramene; AT4G26510.3; AT4G26510.3; AT4G26510.
DR   Gramene; AT4G26510.4; AT4G26510.4; AT4G26510.
DR   KEGG; ath:AT4G26510; -.
DR   Araport; AT4G26510; -.
DR   TAIR; locus:2131498; AT4G26510.
DR   eggNOG; KOG4203; Eukaryota.
DR   eggNOG; COG0035; LUCA.
DR   eggNOG; COG0572; LUCA.
DR   HOGENOM; HOG000262757; -.
DR   InParanoid; O65583; -.
DR   KO; K00876; -.
DR   OMA; YHIVDSH; -.
DR   OrthoDB; 929897at2759; -.
DR   PhylomeDB; O65583; -.
DR   BioCyc; ARA:AT4G26510-MONOMER; -.
DR   UniPathway; UPA00574; UER00636.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
DR   PRO; PR:O65583; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O65583; baseline and differential.
DR   Genevisible; O65583; AT.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IBA:GO_Central.
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:0009116; P:nucleoside metabolic process; IEA:InterPro.
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   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;
DR   PRODOM; O65583.
DR   SWISS-2DPAGE; O65583.
KW   Allosteric enzyme; Glycosyltransferase; GTP-binding; Kinase;
KW   Multifunctional enzyme; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..469
FT                   /note="Uridine kinase-like protein 4"
FT                   /id="PRO_0000120784"
FT   NP_BIND         326..329
FT                   /note="GTP"
FT                   /evidence="ECO:0000250"
FT   REGION          46..249
FT                   /note="Uridine kinase"
FT                   /evidence="ECO:0000250"
FT   REGION          259..469
FT                   /note="Uracil phosphoribosyltransferase"
FT                   /evidence="ECO:0000250"
FT   REGION          392..395
FT                   /note="5-phospho-alpha-D-ribose 1-diphosphate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          457..459
FT                   /note="Uracil binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /note="GTP"
FT                   /evidence="ECO:0000250"
FT   BINDING         292
FT                   /note="GTP"
FT                   /evidence="ECO:0000250"
FT   BINDING         336
FT                   /note="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         361
FT                   /note="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         381
FT                   /note="GTP"
FT                   /evidence="ECO:0000250"
FT   BINDING         387
FT                   /note="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         458
FT                   /note="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        94
FT                   /note="E -> G (in Ref. 5; BAF00520)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   469 AA;  52639 MW;  E5A6357C1DF76BC7 CRC64;
     MGSKSVVDMI EAASRAHFSG LHVNGHMNGL EPSALKETTS ASEDIQRQPF VIGVAGGAAS
     GKTTVCDMII QQLHDQRVVL INLDSFYHNL TEEELARVHE YNFDHPDAFD TEHLLSCMEK
     LRQGQAVDIP KYDFKTYRSS VFRRVNPTDV IILEGILLFH DPRVRKLMNM KIFVCTDADV
     RLARRIKRDT VENGRDIGTV LDQYSKFVKP AFDDFILPTK KYADIIIPRG GDNHVAIDLI
     VQHICTKLGQ HDLCKIYPNL YVIHSTFQIR GMHTLIRDSQ TTKHDFVFYS DRLIRLVVEH
     GLGHLPFTEK QVITPTGCVY SGVDFCKRLC GVSVIRSGES MENALRACCK GIKIGKILIH
     REGDNGQQLV YEKLPNDISE RHVLLLDPIL GTGNSAVEAI NLLISKGVPE GNIIFLNLIS
     APQGVHVVCK KFPRIKIVTS EIDNGLNEEF RVIPGMGEFG DRYFGTDDD
//

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