ID K0ZXV6_9STRE Unreviewed; 212 AA.
AC K0ZXV6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
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 ECO:0000313|EMBL:EKA11840.1};
GN ORFNames=GMD4S_01762 {ECO:0000313|EMBL:EKA11840.1};
OS Streptococcus sp. GMD4S.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1169673 {ECO:0000313|EMBL:EKA11840.1, ECO:0000313|Proteomes:UP000004724};
RN [1] {ECO:0000313|EMBL:EKA11840.1, ECO:0000313|Proteomes:UP000004724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMD4S {ECO:0000313|EMBL:EKA11840.1,
RC ECO:0000313|Proteomes:UP000004724};
RX PubMed=23493677; DOI=10.1101/gr.142208.112;
RA Fitzsimons M.S., Novotny M., Lo C.C., Dichosa A.E., Yee-Greenbaum J.L.,
RA Snook J.P., Gu W., Chertkov O., Davenport K.W., McMurry K., Reitenga K.G.,
RA Daughton A.R., He J., Johnson S.L., Gleasner C.D., Wills P.L.,
RA Parson-Quintana B., Chain P.S., Detter J.C., Lasken R.S., Han C.S.;
RT "Nearly finished genomes produced using gel microdroplet culturing reveal
RT substantial intraspecies genomic diversity within the human microbiome.";
RL Genome Res. 23:878-888(2013).
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:EKA11840.1}.
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DR EMBL; AJRE01000030; EKA11840.1; -; Genomic_DNA.
DR RefSeq; WP_000033393.1; NZ_AJRE01000030.1.
DR AlphaFoldDB; K0ZXV6; -.
DR PATRIC; fig|1169673.3.peg.332; -.
DR Proteomes; UP000004724; 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:EKA11840.1};
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 9..198
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ SEQUENCE 212 AA; 23491 MW; CD30813FDD5EAD99 CRC64;
MSKGFLVSLE GPEGAGKTSV LEALLPILEE NGVEVLTTRE PGGVLIGEKI REVILDPSHT
QMDAKTELLL YIASRRQHLV EKVLPALEAG KLVIMDRFID SSVAYQGFGR GLDIEAIDWL
NHFATDGLKP DLTLYFDIEV EEGLARIAAN SDREVNRLDL EGLDLHKKVR QGYLSLLDKE
GNRIVKIDAS LPLEQVVETT KAVLFDRMGL DK
//
