ID A0A167LLY0_CALVF Unreviewed; 263 AA.
AC A0A167LLY0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 18-JUN-2025, entry version 38.
DE RecName: Full=Uridylate kinase {ECO:0000256|HAMAP-Rule:MF_03172};
DE Short=UK {ECO:0000256|HAMAP-Rule:MF_03172};
DE EC=2.7.4.14 {ECO:0000256|HAMAP-Rule:MF_03172};
DE AltName: Full=ATP:UMP phosphotransferase {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 kinase {ECO:0000256|HAMAP-Rule:MF_03172};
DE Short=UMP kinase {ECO:0000256|HAMAP-Rule:MF_03172};
DE Short=UMPK {ECO:0000256|HAMAP-Rule:MF_03172};
GN ORFNames=CALVIDRAFT_153492 {ECO:0000313|EMBL:KZO95831.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZO95831.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZO95831.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZO95831.1,
RC ECO:0000313|Proteomes:UP000076738};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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
CC dUMP as phosphate acceptors, but can also use CMP, dCMP and AMP.
CC {ECO:0000256|HAMAP-Rule:MF_03172}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UMP + ATP = UDP + ADP; Xref=Rhea:RHEA:24400,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:456216; EC=2.7.4.14;
CC Evidence={ECO:0000256|ARBA:ARBA00048116, 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}. Note=Predominantly
CC cytoplasmic. {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}.
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DR EMBL; KV417287; KZO95831.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167LLY0; -.
DR STRING; 1330018.A0A167LLY0; -.
DR OrthoDB; 442176at2759; -.
DR Proteomes; UP000076738; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004127; F:(d)CMP kinase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; NUCLEOTIDE KINASE; 1.
DR Pfam; PF13207; AAA_17; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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|ARBA:ARBA00022777, 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|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW Rule:MF_03172}; Reference proteome {ECO:0000313|Proteomes:UP000076738};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03172}.
FT REGION 83..113
FT /note="NMPbind"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT REGION 195..205
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 63..68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 89
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 111..113
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 158..161
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 165
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 202
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 213
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
SQ SEQUENCE 263 AA; 28855 MW; E3CC1E4E05584AB4 CRC64;
MPTILDKVQG VFGKKEHAEP ASALQAAALT NAAGITAATE AESTTPAFDH GKVTVIFVLG
GPGAGKGTQC DKLVKDYGFV HLSAGDLLRA EQNRPGSQYG DMIREYIREG KIVPMEVTIK
LLENAMRSAL SARAKEEKGE DKWGAAWAEG RGRFLIDGFP RKMDQAIKFD EDVCKSGFVL
FLSTTEAVLL QRLLERGKTS GREDDNPESI SKRFRTFEET SMPVVEYYRQ RQKVVEIDSS
PPIEEVYAKI RIAVDAALAM VAP
//
