ID A0A078M8K7_9STAP Unreviewed; 209 AA.
AC A0A078M8K7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Thymidylate kinase {ECO:0000256|HAMAP-Rule:MF_00165};
DE EC=2.7.4.9 {ECO:0000256|HAMAP-Rule:MF_00165};
DE AltName: Full=dTMP kinase {ECO:0000256|HAMAP-Rule:MF_00165};
GN Name=tmk_2 {ECO:0000313|EMBL:CEA02605.1};
GN Synonyms=tmk {ECO:0000256|HAMAP-Rule:MF_00165};
GN ORFNames=BN1048_01778 {ECO:0000313|EMBL:CEA02605.1};
OS Jeotgalicoccus saudimassiliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Jeotgalicoccus.
OX NCBI_TaxID=1461582 {ECO:0000313|EMBL:CEA02605.1, ECO:0000313|Proteomes:UP000044136};
RN [1] {ECO:0000313|EMBL:CEA02605.1, ECO:0000313|Proteomes:UP000044136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13MG44_air {ECO:0000313|EMBL:CEA02605.1,
RC ECO:0000313|Proteomes:UP000044136};
RA Urmite Genomes Urmite Genomes;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC salvage pathways of dTTP synthesis. {ECO:0000256|HAMAP-Rule:MF_00165}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528,
CC ChEBI:CHEBI:456216; EC=2.7.4.9;
CC Evidence={ECO:0000256|ARBA:ARBA00001008, ECO:0000256|HAMAP-
CC Rule:MF_00165};
CC -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC {ECO:0000256|ARBA:ARBA00009776, ECO:0000256|HAMAP-Rule:MF_00165}.
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DR EMBL; CCSE01000001; CEA02605.1; -; Genomic_DNA.
DR RefSeq; WP_035810378.1; NZ_CCSE01000001.1.
DR AlphaFoldDB; A0A078M8K7; -.
DR STRING; 1461582.BN1048_01778; -.
DR eggNOG; COG0125; Bacteria.
DR HOGENOM; CLU_049131_0_2_9; -.
DR OrthoDB; 9774907at2; -.
DR Proteomes; UP000044136; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01672; TMPK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00165; Thymidylate_kinase; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039430; Thymidylate_kin-like_dom.
DR InterPro; IPR018095; Thymidylate_kin_CS.
DR InterPro; IPR018094; Thymidylate_kinase.
DR NCBIfam; TIGR00041; DTMP_kinase; 1.
DR PANTHER; PTHR10344; THYMIDYLATE KINASE; 1.
DR PANTHER; PTHR10344:SF4; THYMIDYLATE KINASE; 1.
DR Pfam; PF02223; Thymidylate_kin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00165};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:CEA02605.1};
KW Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727, ECO:0000256|HAMAP-
KW Rule:MF_00165};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00165}; Reference proteome {ECO:0000313|Proteomes:UP000044136};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00165}.
FT DOMAIN 7..194
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
FT BINDING 9..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ SEQUENCE 209 AA; 23726 MW; EF57D5DCE6C07F1E CRC64;
MSYFITFEGP EGSGKTTVIE QIRALLAKTH EVVKTREPGG IPISEKIREV ILTKEHDMDG
RTEALLFAAS RRQHLVERVV PALESGKIVL CDRFIDSSLA YQGIARGIGF DDIMAVNKFA
IEHHMPDLTI YLKLDPETGL QRIRDNAREN NRLDDETMDF HKKVVLGYNE LSELYPDRIK
IVDAAQSVED VVRDTLNIIN TYIQSRGEE
//
