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KCY_XENLA
ID   KCY_XENLA               Reviewed;         193 AA.
AC   Q7ZX23; Q7SY80;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=UMP-CMP kinase {ECO:0000255|HAMAP-Rule:MF_03172};
DE            EC=2.7.4.14 {ECO:0000255|HAMAP-Rule:MF_03172};
DE   AltName: Full=Deoxycytidylate kinase {ECO:0000255|HAMAP-Rule:MF_03172};
DE            Short=CK {ECO:0000255|HAMAP-Rule:MF_03172};
DE            Short=dCMP kinase {ECO:0000255|HAMAP-Rule:MF_03172};
DE   AltName: Full=Nucleoside-diphosphate kinase {ECO:0000255|HAMAP-Rule:MF_03172};
DE            EC=2.7.4.6 {ECO:0000255|HAMAP-Rule:MF_03172};
DE   AltName: Full=Uridine monophosphate/cytidine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_03172};
DE            Short=UMP/CMP kinase {ECO:0000255|HAMAP-Rule:MF_03172};
DE            Short=UMP/CMPK {ECO:0000255|HAMAP-Rule:MF_03172};
GN   Name=cmpk1; Synonyms=cmpk;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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. Also displays broad nucleoside diphosphate
CC       kinase activity. {ECO:0000255|HAMAP-Rule:MF_03172}.
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};
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};
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};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC         deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC         ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03172};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC         triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03172};
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: Nucleus {ECO:0000255|HAMAP-Rule:MF_03172}.
CC       Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03172}. Note=Predominantly
CC       nuclear. {ECO:0000255|HAMAP-Rule:MF_03172}.
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 dissambling the active center
CC       during each catalytic cycle provides an effective means to prevent ATP
CC       hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03172}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. UMP-CMP kinase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03172}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH45275.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH54975.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC045275; AAH45275.1; ALT_INIT; mRNA.
DR   EMBL; BC054975; AAH54975.2; ALT_INIT; mRNA.
DR   RefSeq; NP_001082709.1; NM_001089240.1.
DR   AlphaFoldDB; Q7ZX23; -.
DR   SMR; Q7ZX23; -.
DR   DNASU; 398670; -.
DR   GeneID; 398670; -.
DR   KEGG; xla:398670; -.
DR   CTD; 398670; -.
DR   Xenbase; XB-GENE-980044; cmpk1.S.
DR   OrthoDB; 1378291at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 398670; Expressed in zone of skin and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0036430; F:CMP kinase activity; IEA:RHEA.
DR   GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; ISS:UniProtKB.
DR   GO; GO:0033862; F:UMP kinase activity; IEA:RHEA.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0006165; P:nucleoside diphosphate phosphorylation; ISS:UniProtKB.
DR   GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule.
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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW   Pyrimidine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..193
FT                   /note="UMP-CMP kinase"
FT                   /id="PRO_0000292026"
FT   REGION          33..63
FT                   /note="NMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   REGION          133..143
FT                   /note="LID"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         13..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         39
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         61..63
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         93..96
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         100
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         134
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         140
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         151
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   CONFLICT        116
FT                   /note="F -> I (in Ref. 1; AAH54975)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   193 AA;  22106 MW;  B2BD9C8638D86360 CRC64;
     MKPLVVFVLG GPGAGKGTQC ERIVQKYGYT HLSAGDLLRD ERKKPDSQYG ELIESYIRDG
     KIVPVEITIS LLQRAMERTM AFDANKHKFL IDGFPRNEDN LQGWERTMNG KADVSFVLFF
     DCDNETCIER CLERGKSSGR SDDNRESLEK RIQTYLQSTR PIIDLYEKRG KVRKVDASKS
     VDEVFTKVQN IFD
 
 
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