UCKA_DICDI
ID UCKA_DICDI Reviewed; 499 AA.
AC Q55EL3; Q6S4W3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Uridine-cytidine kinase A;
DE EC=2.7.1.48;
DE AltName: Full=Cytidine monophosphokinase A;
DE AltName: Full=Uridine kinase/uracil phosphoribosyltransferase;
DE Short=UK-UPRT;
DE AltName: Full=Uridine monophosphokinase A;
GN Name=udkA; Synonyms=ukuprt; ORFNames=DDB_G0269034;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-493.
RX PubMed=14973196; DOI=10.1073/pnas.0304686101;
RA Striepen B., Pruijssers A.J.P., Huang J., Li C., Gubbels M.-J.,
RA Umejiego N.N., Hedstrom L., Kissinger J.C.;
RT "Gene transfer in the evolution of parasite nucleotide biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:3154-3159(2004).
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; AAFI02000004; EAL73106.1; -; Genomic_DNA.
DR EMBL; AY466382; AAS47702.1; -; Genomic_DNA.
DR RefSeq; XP_647007.1; XM_641915.1.
DR AlphaFoldDB; Q55EL3; -.
DR SMR; Q55EL3; -.
DR STRING; 44689.DDB0216233; -.
DR PaxDb; Q55EL3; -.
DR EnsemblProtists; EAL73106; EAL73106; DDB_G0269034.
DR GeneID; 8616700; -.
DR KEGG; ddi:DDB_G0269034; -.
DR dictyBase; DDB_G0269034; udkA.
DR eggNOG; KOG4203; Eukaryota.
DR HOGENOM; CLU_021278_0_3_1; -.
DR InParanoid; Q55EL3; -.
DR OMA; RTKTMYG; -.
DR PhylomeDB; Q55EL3; -.
DR Reactome; R-DDI-196807; Nicotinate metabolism.
DR Reactome; R-DDI-73614; Pyrimidine salvage.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR PRO; PR:Q55EL3; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004849; F:uridine kinase activity; ISS:dictyBase.
DR GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0008655; P:pyrimidine-containing compound salvage; ISS:dictyBase.
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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..499
FT /note="Uridine-cytidine kinase A"
FT /id="PRO_0000327604"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78..85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 499 AA; 55797 MW; C20ADC62FE55F051 CRC64;
MSDNSTTKVT TNDSPSLTTT TSTTTAPTTT TTTTTTPTHN HDTTIAPGVV KKVYTSGRPP
WYDSKGNLKN PLVIGVCGGS ASGKTTVCDK IIANLNVRWV VLLSMDSFYK NLSKDNDPSK
YNFDHPNAFD YDLMVKTISE LRAGKKVNIP KYCFKTHSRL VHQDTVYGAD VIILEGILTL
YSKELRDLMD IKIFIDTDDD VRLARRLKRD IAERGRTLES VLHQYNTFVK PSFDDYIIPL
KKYADIIVPR GSDNIVAINL LTNHIRLKLK ERGFDPEKTA QLDLEGLELP SSIHVIKETN
QIKAMLSILR NKDTKVGDFV FYSDRLCSLI IEEALTYLPF TEKIVTTPTG SLYHGEELNS
RICALVVLRA GGCMEQPLRS ICKGIRTGKV LIQSDEMKKP HLFYEKLPNV TDSHVLVLDP
TIATGASSEM AIRVLLDHGV PENKIIFVSV IASLKGILYL NYRFPDVQFV VSAIDKELSD
EGFILPGCGF YSNRYFGTH
