UCK2A_DANRE
ID UCK2A_DANRE Reviewed; 261 AA.
AC Q7SYM0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Uridine-cytidine kinase 2-A;
DE Short=UCK 2-A;
DE EC=2.7.1.48 {ECO:0000250|UniProtKB:Q9BZX2};
DE AltName: Full=Cytidine monophosphokinase 2-A;
DE AltName: Full=Uridine monophosphokinase 2-A;
GN Name=uck2a; ORFNames=si:ch211-216k22.2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylates uridine and cytidine to uridine monophosphate
CC and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides
CC or purine ribonucleosides. Can use ATP or GTP as a phosphate donor.
CC {ECO:0000250|UniProtKB:Q9BZX2}.
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 Evidence={ECO:0000250|UniProtKB:Q9BZX2};
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 Evidence={ECO:0000250|UniProtKB:Q9BZX2};
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC CTP from cytidine: step 1/3. {ECO:0000250|UniProtKB:Q9BZX2}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uridine: step 1/1. {ECO:0000250|UniProtKB:Q9BZX2}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9BZX2}.
CC -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX927144; CAQ13314.1; -; Genomic_DNA.
DR EMBL; BC054665; AAH54665.1; -; mRNA.
DR RefSeq; NP_001164538.1; NM_001171067.1.
DR AlphaFoldDB; Q7SYM0; -.
DR SMR; Q7SYM0; -.
DR STRING; 7955.ENSDARP00000018636; -.
DR PaxDb; Q7SYM0; -.
DR Ensembl; ENSDART00000002186; ENSDARP00000018636; ENSDARG00000006074.
DR Ensembl; ENSDART00000172134; ENSDARP00000140822; ENSDARG00000109414.
DR GeneID; 100005763; -.
DR KEGG; dre:100005763; -.
DR CTD; 100005763; -.
DR ZFIN; ZDB-GENE-030131-7158; uck2a.
DR eggNOG; KOG4203; Eukaryota.
DR GeneTree; ENSGT01020000230412; -.
DR HOGENOM; CLU_021278_1_1_1; -.
DR InParanoid; Q7SYM0; -.
DR OMA; XLRDISE; -.
DR OrthoDB; 929897at2759; -.
DR PhylomeDB; Q7SYM0; -.
DR TreeFam; TF316686; -.
DR Reactome; R-DRE-73614; Pyrimidine salvage.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR PRO; PR:Q7SYM0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 8.
DR Bgee; ENSDARG00000006074; Expressed in blastula and 28 other tissues.
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:0043771; F:cytidine kinase activity; ISS:UniProtKB.
DR GO; GO:0004849; F:uridine kinase activity; ISS:UniProtKB.
DR GO; GO:0044211; P:CTP salvage; ISS:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0044206; P:UMP salvage; ISS:UniProtKB.
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; IPR029925; UCK-2.
DR InterPro; IPR000764; Uridine_kinase-like.
DR PANTHER; PTHR10285:SF131; PTHR10285:SF131; 1.
DR Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00235; udk; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..261
FT /note="Uridine-cytidine kinase 2-A"
FT /id="PRO_0000346104"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
SQ SEQUENCE 261 AA; 29628 MW; 460C3C02A024490B CRC64;
MAGDSDSKLD NHAENEHVDW QPFLIGVAGG TASGKSSVCG KIMELLGQNK IDHHQRQVAI
LSQDSFYRVL TPEQKAKALK GQFNFDHPDA FDNELIVKTL CEIMEGRTVQ IPVYDFVTHS
RKEETVTVYP ADVVLFEGIL MFYSQEIRDL FQMKLFVDTD ADTRLSRRVL RDISERGRDL
EQVLNQYITF VKPAFEEFCL PTKKYADVII PRGADNLVAI NLIVQHIQDF LNGGLTKRLN
GCLNGHTPRK RHPSESSSRP H
