ID   A0A8J5IKC9_9STRA        Unreviewed;       198 AA.
AC   A0A8J5IKC9;
DT   25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 1.
DT   22-FEB-2023, entry version 5.
DE   RecName: Full=UMP-CMP kinase {ECO:0000256|HAMAP-Rule:MF_03172};
DE            EC=2.7.4.14 {ECO:0000256|HAMAP-Rule:MF_03172};
DE   AltName: Full=Deoxycytidylate kinase {ECO:0000256|HAMAP-Rule:MF_03172};
DE            Short=CK {ECO:0000256|HAMAP-Rule:MF_03172};
DE            Short=dCMP kinase {ECO:0000256|HAMAP-Rule:MF_03172};
DE   AltName: Full=Uridine monophosphate/cytidine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_03172};
DE            Short=UMP/CMP kinase {ECO:0000256|HAMAP-Rule:MF_03172};
DE            Short=UMP/CMPK {ECO:0000256|HAMAP-Rule:MF_03172};
GN   ORFNames=JG688_00009864 {ECO:0000313|EMBL:KAG6959928.1};
OS   Phytophthora aleatoria.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=2496075 {ECO:0000313|EMBL:KAG6959928.1, ECO:0000313|Proteomes:UP000709295};
RN   [1] {ECO:0000313|EMBL:KAG6959928.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NZFS 4037 {ECO:0000313|EMBL:KAG6959928.1};
RA   Mcdougal R., Panda P., Williams N., Studholme D.J.;
RT   "Phytophthora aleatoria, a newly-described species from Pinus radiata is
RT   distinct from Phytophthora cactorum isolates based on comparative
RT   genomics.";
RL   Submitted (JAN-2021) 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. {ECO:0000256|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:0000256|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:0000256|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:0000256|HAMAP-
CC         Rule:MF_03172};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03172};
CC       Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000256|HAMAP-Rule:MF_03172};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03172}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03172}.
CC       Nucleus {ECO:0000256|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:0000256|HAMAP-Rule:MF_03172}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. UMP-CMP kinase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_03172}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03172}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAG6959928.1}.
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; JAENGY010000589; KAG6959928.1; -; Genomic_DNA.
DR   Proteomes; UP000709295; Unassembled WGS sequence.
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:0004127; F:cytidylate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009041; F:uridylate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR006266; UMP_CMP_kinase.
DR   PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR   PANTHER; PTHR23359:SF206; UMP-CMP KINASE; 1.
DR   Pfam; PF00406; ADK; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03172};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03172};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_03172};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03172};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03172};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03172};
KW   Reference proteome {ECO:0000313|Proteomes:UP000709295};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03172}.
FT   REGION          132..142
FT                   /note="LID"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT   BINDING         17..22
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT   BINDING         43
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT   BINDING         64..66
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT   BINDING         91..94
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT   BINDING         98
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT   BINDING         133
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT   BINDING         139
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT   BINDING         150
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT   BINDING         178
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
SQ   SEQUENCE   198 AA;  22071 MW;  20453A06F157C290 CRC64;
     MSATLAKKIL FVLGGPGAGK GTQCAKLVEK YGFVHLSAGD LLREERQSGS ENGELIDRMI
     KEGQIVPVKI TLNLLQQAMV KSGRDLFLID GFPRNFDNLQ GWQEEMAEDE FQVQGVLFYD
     CPEGVMEERL LERGKTSGRT DDNAEAIRKR FRTYLDSTMP VIMHYEKQNK VFKVDATPGP
     DEVFEATAAL IGPLVADK
//