ID A0A256BPG3_9LACT Unreviewed; 220 AA.
AC A0A256BPG3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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 {ECO:0000256|HAMAP-Rule:MF_00165};
GN ORFNames=B9P78_02525 {ECO:0000313|EMBL:OYQ67695.1};
OS Aerococcus sp. 1KP-2016.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus.
OX NCBI_TaxID=1981982 {ECO:0000313|EMBL:OYQ67695.1, ECO:0000313|Proteomes:UP000215823};
RN [1] {ECO:0000313|EMBL:OYQ67695.1, ECO:0000313|Proteomes:UP000215823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1KP-2016 {ECO:0000313|EMBL:OYQ67695.1,
RC ECO:0000313|Proteomes:UP000215823};
RA Chaplin A.V., Chagina I.A., Rubalsky E.O., Gadua N.T., Borisova O.Y.,
RA Kafarskaia L.I., Karagaltseva N.M., Kocherovets V.I., Afanas'Ev S.,
RA Aleshkin V.A.;
RT "Aerococcus sp. 1KP-2016, a novel member of genus Aerococcus.";
RL Submitted (APR-2017) 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}.
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:OYQ67695.1}.
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DR EMBL; NEEY01000007; OYQ67695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A256BPG3; -.
DR OrthoDB; 9774907at2; -.
DR Proteomes; UP000215823; 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:OYQ67695.1};
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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00165}.
FT DOMAIN 13..205
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
FT BINDING 15..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ SEQUENCE 220 AA; 24326 MW; 2B3ED6043025478B CRC64;
MDTEQLLGKF ITVEGPDGAG KTTLINGLTA KLEASLNVPL ILTREPGGDP IAEQIRRIIL
DPANTDLDPR AEALLYAASR RQHLVHTVLP ALAAGQLVLC DRFVDSSIAY QGYGREIGEE
GILAINAFAT DGRQPDLTLY LDISAEEGIR RIQANRSQAD QNRLDVETID FHQRVHQGYQ
VLRAQYPDRI QVIDATQSPE AMQAEALRIV QAHFPQFFSN
//
