KCY2_CAEEL
ID KCY2_CAEEL Reviewed; 191 AA.
AC Q20230;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=UMP-CMP kinase 2 {ECO:0000255|HAMAP-Rule:MF_03172};
DE EC=2.7.4.14 {ECO:0000255|HAMAP-Rule:MF_03172};
DE AltName: Full=Deoxycytidylate kinase 2 {ECO:0000255|HAMAP-Rule:MF_03172};
DE Short=CK 2 {ECO:0000255|HAMAP-Rule:MF_03172};
DE Short=dCMP kinase 2 {ECO:0000255|HAMAP-Rule:MF_03172};
DE AltName: Full=Uridine monophosphate/cytidine monophosphate kinase 2 {ECO:0000255|HAMAP-Rule:MF_03172};
DE Short=UMP/CMP kinase 2 {ECO:0000255|HAMAP-Rule:MF_03172};
DE Short=UMP/CMPK 2 {ECO:0000255|HAMAP-Rule:MF_03172};
GN ORFNames=F40F8.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=19645718; DOI=10.1111/j.1742-4658.2009.07168.x;
RA Kim S., Park D.H., Kim T.H., Hwang M., Shim J.;
RT "Functional analysis of pyrimidine biosynthesis enzymes using the
RT anticancer drug 5-fluorouracil in Caenorhabditis elegans.";
RL FEBS J. 276:4715-4726(2009).
CC -!- FUNCTION: Catalyzes the phosphorylation of pyrimidine nucleoside
CC monophosphates at the expense of ATP. Plays an important role in de
CC novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP
CC as phosphate acceptors. {ECO:0000255|HAMAP-Rule:MF_03172,
CC ECO:0000269|PubMed:19645718}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03172, ECO:0000269|PubMed:19645718};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593,
CC ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03172, ECO:0000269|PubMed:19645718};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + UMP = ADP + UDP; Xref=Rhea:RHEA:24400,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03172, ECO:0000269|PubMed:19645718};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03172};
CC Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000255|HAMAP-Rule:MF_03172};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03172}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03172}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03172}.
CC -!- TISSUE SPECIFICITY: Expressed in neurons and the pharynx.
CC {ECO:0000269|PubMed:19645718}.
CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two
CC small peripheral domains, NMPbind and LID, which undergo movements
CC during catalysis. The LID domain closes over the site of phosphoryl
CC transfer upon ATP binding. Assembling and disassembling the active
CC center during each catalytic cycle provides an effective means to
CC prevent ATP hydrolysis (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: In contrast to its homolog C29F7.3, does not
CC confer resistance to 5-fluorouracil. {ECO:0000269|PubMed:19645718}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. UMP-CMP kinase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03172}.
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DR EMBL; Z69302; CAA93264.1; -; Genomic_DNA.
DR PIR; T22036; T22036.
DR RefSeq; NP_496386.1; NM_063985.5.
DR AlphaFoldDB; Q20230; -.
DR SMR; Q20230; -.
DR BioGRID; 40011; 7.
DR STRING; 6239.F40F8.1.1; -.
DR EPD; Q20230; -.
DR PaxDb; Q20230; -.
DR PeptideAtlas; Q20230; -.
DR EnsemblMetazoa; F40F8.1a.1; F40F8.1a.1; WBGene00009575.
DR UCSC; F40F8.1.1; c. elegans.
DR WormBase; F40F8.1a; CE05842; WBGene00009575; -.
DR eggNOG; KOG3079; Eukaryota.
DR GeneTree; ENSGT00940000163540; -.
DR HOGENOM; CLU_032354_0_2_1; -.
DR InParanoid; Q20230; -.
DR PhylomeDB; Q20230; -.
DR Reactome; R-CEL-499943; Interconversion of nucleotide di- and triphosphates.
DR PRO; PR:Q20230; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00009575; Expressed in adult organism and 4 other tissues.
DR ExpressionAtlas; Q20230; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0036430; F:CMP kinase activity; IEA:RHEA.
DR GO; GO:0004127; F:cytidylate kinase activity; IBA:GO_Central.
DR GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA.
DR GO; GO:0033862; F:UMP kinase activity; IDA:WormBase.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0046705; P:CDP biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006225; P:UDP biosynthetic process; IDA:WormBase.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR HAMAP; MF_03172; Adenylate_kinase_UMP_CMP_kin; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006266; UMP_CMP_kinase.
DR PANTHER; PTHR23359; PTHR23359; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01359; UMP_CMP_kin_fam; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Pyrimidine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..191
FT /note="UMP-CMP kinase 2"
FT /id="PRO_0000422253"
FT REGION 32..62
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT REGION 128..136
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT BINDING 12..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT BINDING 38
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT BINDING 60..62
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT BINDING 88..91
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT BINDING 95
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT BINDING 129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT BINDING 133
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT BINDING 144
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT BINDING 172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
SQ SEQUENCE 191 AA; 21240 MW; 8D65F13456BC6790 CRC64;
MHNVVFVLGP PGSGKGTICA KIQENLNYVH LSAGDLLRAE RQREGSEFGA LIESHIKNGS
IVPVEITCSL LENAMKACGD AKGFLVDGFP RNEDNLQGWN KQMDGKALVQ FVLFLSCPVS
ICIERCLNRG QGRTDDNEES LKKRVETYNQ QTFPIIEHFE KSGLVREVKS ERPVDVVYAD
VEKVFDAANK K
