KCY1_CAEEL
ID KCY1_CAEEL Reviewed; 191 AA.
AC O17622;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=UMP-CMP kinase 1 {ECO:0000255|HAMAP-Rule:MF_03172};
DE EC=2.7.4.14 {ECO:0000255|HAMAP-Rule:MF_03172};
DE AltName: Full=Deoxycytidylate kinase 1 {ECO:0000255|HAMAP-Rule:MF_03172};
DE Short=CK 1 {ECO:0000255|HAMAP-Rule:MF_03172};
DE Short=dCMP kinase 1 {ECO:0000255|HAMAP-Rule:MF_03172};
DE AltName: Full=Uridine monophosphate/cytidine monophosphate kinase 1 {ECO:0000255|HAMAP-Rule:MF_03172};
DE Short=UMP/CMP kinase 1 {ECO:0000255|HAMAP-Rule:MF_03172};
DE Short=UMP/CMPK 1 {ECO:0000255|HAMAP-Rule:MF_03172};
GN ORFNames=C29F7.3;
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 the hypodermis, intestine, and
CC pharynx. {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: Confers resistance to 5-fluorouracil.
CC {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; Z92827; CAB07328.1; -; Genomic_DNA.
DR PIR; T19573; T19573.
DR RefSeq; NP_510236.1; NM_077835.3.
DR AlphaFoldDB; O17622; -.
DR SMR; O17622; -.
DR BioGRID; 46367; 12.
DR STRING; 6239.C29F7.3; -.
DR EPD; O17622; -.
DR PaxDb; O17622; -.
DR PeptideAtlas; O17622; -.
DR EnsemblMetazoa; C29F7.3.1; C29F7.3.1; WBGene00007812.
DR GeneID; 181464; -.
DR KEGG; cel:CELE_C29F7.3; -.
DR UCSC; C29F7.3; c. elegans.
DR CTD; 181464; -.
DR WormBase; C29F7.3; CE08444; WBGene00007812; -.
DR eggNOG; KOG3079; Eukaryota.
DR GeneTree; ENSGT00940000163540; -.
DR HOGENOM; CLU_032354_0_2_1; -.
DR InParanoid; O17622; -.
DR OMA; RFQFTHL; -.
DR OrthoDB; 1378291at2759; -.
DR PhylomeDB; O17622; -.
DR PRO; PR:O17622; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00007812; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
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 1"
FT /id="PRO_0000422252"
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; 21202 MW; 8920CE3F444FBC60 CRC64;
MYNVVFVLGP PGSGKGTICT QIHENLGYVH LSAGDLLRAE RERAGSEYGA LIEGHIKNGS
IVPVEITCAL LENAMIASKD ANGFLIDGFP RNEDNWSGWN KQMGGKVNEQ FVLFLSCPVD
VCIDRCLHRG QGRTDDNVES LKKRVETYNQ STFPIIEHFE KVGMVREVNS ERPVTEVYED
VVKVFAAANQ K
