UCK_DROME
ID UCK_DROME Reviewed; 260 AA.
AC Q9VC99; H1UUH6;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Uridine-cytidine kinase {ECO:0000312|FlyBase:FBgn0263398};
DE Short=UCK {ECO:0000312|FlyBase:FBgn0263398};
DE EC=2.7.1.48;
DE AltName: Full=Cytidine monophosphokinase;
DE AltName: Full=Uridine monophosphokinase;
GN Name=Uck {ECO:0000312|FlyBase:FBgn0263398};
GN Synonyms=CR42873 {ECO:0000312|FlyBase:FBgn0263398};
GN ORFNames=CG6364 {ECO:0000312|FlyBase:FBgn0263398};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION (MICROBIAL INFECTION), AND DISRUPTION PHENOTYPE (MICROBIAL
RP INFECTION).
RX PubMed=22851751; DOI=10.1128/iai.00670-12;
RA Von Ohlen T., Luce-Fedrow A., Ortega M.T., Ganta R.R., Chapes S.K.;
RT "Identification of critical host mitochondrion-associated genes during
RT Ehrlichia chaffeensis infections.";
RL Infect. Immun. 80:3576-3586(2012).
RN [5]
RP FUNCTION (MICROBIAL INFECTION), AND DISRUPTION PHENOTYPE (MICROBIAL
RP INFECTION).
RX PubMed=23306065; DOI=10.1016/j.ijmm.2012.12.002;
RA Drolia R., Von Ohlen T., Chapes S.K.;
RT "Ehrlichia chaffeensis replication sites in adult Drosophila
RT melanogaster.";
RL Int. J. Med. Microbiol. 303:40-49(2013).
CC -!- FUNCTION: (Microbial infection) Required for optimal replication of
CC E.chaffeensis in the immune tissues, hemocytes, and fat body.
CC {ECO:0000269|PubMed:22851751, ECO:0000269|PubMed:23306065}.
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 -!- 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 -!- 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 -!- DISRUPTION PHENOTYPE: (Microbial infection) After infection with
CC E.chaffeensis, results in reduced bacterial replication rate and
CC increased survival (PubMed:22851751). RNAi-mediated knockdown in the
CC whole organism, in the fat body or hemocytes results in a similar
CC phenotype to the genetic knockout (PubMed:23306065). However, knockdown
CC in the eye, salivary gland or wing has no effect (PubMed:23306065).
CC {ECO:0000269|PubMed:22851751, ECO:0000269|PubMed:23306065}.
CC -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000305}.
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DR EMBL; AE014297; AAF56274.1; -; Genomic_DNA.
DR EMBL; AE014297; AFH06599.1; -; Genomic_DNA.
DR EMBL; AE014297; AFH06600.1; -; Genomic_DNA.
DR EMBL; AE014297; AFH06601.1; -; Genomic_DNA.
DR EMBL; BT133061; AEX93146.1; -; mRNA.
DR RefSeq; NP_001247281.1; NM_001260352.2.
DR RefSeq; NP_001247282.1; NM_001260353.2.
DR RefSeq; NP_001247283.1; NM_001260354.2.
DR RefSeq; NP_651241.1; NM_142984.2.
DR AlphaFoldDB; Q9VC99; -.
DR SMR; Q9VC99; -.
DR STRING; 7227.FBpp0288805; -.
DR EnsemblMetazoa; FBtr0084602; FBpp0083986; FBgn0263398.
DR EnsemblMetazoa; FBtr0309095; FBpp0301103; FBgn0263398.
DR EnsemblMetazoa; FBtr0309096; FBpp0301104; FBgn0263398.
DR EnsemblMetazoa; FBtr0309097; FBpp0301105; FBgn0263398.
DR GeneID; 42894; -.
DR KEGG; dme:Dmel_CG6364; -.
DR UCSC; CG6364-RA; d. melanogaster.
DR CTD; 42894; -.
DR FlyBase; FBgn0263398; Uck.
DR VEuPathDB; VectorBase:FBgn0263398; -.
DR eggNOG; KOG4203; Eukaryota.
DR GeneTree; ENSGT01020000230412; -.
DR InParanoid; Q9VC99; -.
DR OMA; WGEISNN; -.
DR OrthoDB; 929897at2759; -.
DR PhylomeDB; Q9VC99; -.
DR Reactome; R-DME-73614; Pyrimidine salvage.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR BioGRID-ORCS; 42894; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42894; -.
DR PRO; PR:Q9VC99; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0263398; Expressed in mouthpart and 35 other tissues.
DR ExpressionAtlas; Q9VC99; baseline and differential.
DR Genevisible; Q9VC99; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd02023; UMPK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006083; PRK/URK.
DR InterPro; IPR029920; UCK-1.
DR InterPro; IPR000764; Uridine_kinase-like.
DR PANTHER; PTHR10285:SF66; PTHR10285:SF66; 1.
DR Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..260
FT /note="Uridine-cytidine kinase"
FT /id="PRO_0000164458"
FT BINDING 34..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 260 AA; 29213 MW; 2EE57423704925E6 CRC64;
MQDLRNADTL RLPNGDGAAA NDEVKSPFLI GVAGGTASGK STVCKKIMEQ LGQAEMDHTQ
RQVVSISQDS FYRELTPAEK AKAQKGLFNF DHPDAFNEEL MYSTLQNILK GHKVEIPSYD
YRTNSLDFEN VLVIYPADVV LFEGILVFYF PKIRELFHMK LFVDTDSDTR LARRVPRDIN
ERGRDLDAVL TQYMTFVKPA FEEFCSPTKK FADVIIPRGA DNTVAIDLIV HHIGEILATT
NSAQHSNTVR VAASSMKRDH
