UCKC_DICDI
ID UCKC_DICDI Reviewed; 449 AA.
AC Q54R62;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Uridine-cytidine kinase C;
DE EC=2.7.1.48;
DE AltName: Full=Cytidine monophosphokinase C;
DE AltName: Full=Uridine monophosphokinase C;
GN Name=udkC; ORFNames=DDB_G0283371;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes the conversion of uridine into uridine
CC monophosphate and cytidine into cytidine monophosphate in the
CC pyrimidine salvage pathway. {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000054; EAL65762.1; -; Genomic_DNA.
DR RefSeq; XP_639121.1; XM_634029.1.
DR AlphaFoldDB; Q54R62; -.
DR SMR; Q54R62; -.
DR STRING; 44689.DDB0231239; -.
DR PaxDb; Q54R62; -.
DR EnsemblProtists; EAL65762; EAL65762; DDB_G0283371.
DR GeneID; 8624054; -.
DR KEGG; ddi:DDB_G0283371; -.
DR dictyBase; DDB_G0283371; udkC.
DR eggNOG; KOG4203; Eukaryota.
DR HOGENOM; CLU_028566_0_0_1; -.
DR InParanoid; Q54R62; -.
DR OMA; YEIGTIM; -.
DR PhylomeDB; Q54R62; -.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR PRO; PR:Q54R62; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:UniProt.
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 Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR033469; CYTH-like_dom_sf.
DR InterPro; IPR023577; CYTH_domain.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006083; PRK/URK.
DR Pfam; PF01928; CYTH; 1.
DR Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55154; SSF55154; 1.
DR PROSITE; PS51707; CYTH; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..449
FT /note="Uridine-cytidine kinase C"
FT /id="PRO_0000371326"
FT DOMAIN 235..401
FT /note="CYTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01044"
FT BINDING 58..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 449 AA; 50738 MW; 5778E8C9A9EE867B CRC64;
MDSLEIEVIP RPDKDDRYTI KPLKDTLSFD KGFFLAVRAI QSIRKKSQGS VIVVGIAGPS
GAGKTSIAQK IVSVLPKSIL ISLDNYLDSS RQIIEENYDD YRLVDFELLK KNISDLISNK
PTDLPLYDFT KSGRYAYKRV QPPESKVLLI EGIYALHEEI RHLLDLRVSI SGGVHFDLIK
RIFRDVHRTG QQPHESLQQI TDTVYPMYKA FIEPDLQLAE IQVVNKFNPF GGLLNPIYIL
KSVKQGVTVD MIHSVLNKST IQENTARYYD IYLIPPNTTF ANSSSCDWIR VRNADGQYSI
MFSEEIKEGP FIISPRVDFV VGVNMLGGLM SLGYQMVAII HRKSTIFKDG KIIISYDELE
ELGQTFVQIK GFDATSVQEA GKKLGLENNY LQKSYIELYQ DKYKKSLSDN STVTTLPIGG
INNNNTINNN NNNNNNNNLS LSNFINSKL