ID A0A367LM12_9HYPO Unreviewed; 233 AA.
AC A0A367LM12;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=L249_3537 {ECO:0000313|EMBL:RCI15475.1};
OS Ophiocordyceps polyrhachis-furcata BCC 54312.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI15475.1, ECO:0000313|Proteomes:UP000253664};
RN [1] {ECO:0000313|EMBL:RCI15475.1, ECO:0000313|Proteomes:UP000253664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI15475.1,
RC ECO:0000313|Proteomes:UP000253664};
RX PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT pathogenicity and host specificity in insect fungi.";
RL BMC Genomics 16:881-881(2015).
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=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;
CC Evidence={ECO:0000256|ARBA:ARBA00001331, 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|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC 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}.
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:RCI15475.1}.
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; LKCN02000002; RCI15475.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367LM12; -.
DR STRING; 1330021.A0A367LM12; -.
DR Proteomes; UP000253664; 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-EC.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 NCBIfam; TIGR01359; UMP_CMP_kin_fam; 1.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR PANTHER; PTHR23359:SF206; UMP-CMP KINASE; 1.
DR Pfam; PF00406; ADK; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03172};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000253664};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03172}.
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..93
FT /note="NMPbind"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT REGION 166..176
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT COMPBIAS 8..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 69
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 91..93
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 129..132
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 136
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 173
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 184
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
SQ SEQUENCE 233 AA; 25671 MW; 0021E85053CE6E34 CRC64;
MPPPPSTTTD NNNQQQLPPP SSSSSAAFTP DKATVVFVLG GPGAGKGTQC SRLVSQYGFT
HLSAGDLLRA EQDRPGSQFG DLIRTHIKEG LIVPMEVTVQ LLENAMLEAL NNNNNNNKQK
GPARFLIDGF PRKLDQAYRF ESAICNPSLV LFYDCPENVM QDRLLERGKT SGRDDDNAES
ILKRFRTFVD TSMPVVDHYD KKGCVVKVDA THDPDAVFAE TQKRLKEKLG DGF
//
