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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
 
 
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