ID R7LHH0_9CLOT Unreviewed; 210 AA.
AC R7LHH0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=BN768_00262 {ECO:0000313|EMBL:CDE88125.1};
OS Clostridium sp. CAG:729.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262835 {ECO:0000313|EMBL:CDE88125.1, ECO:0000313|Proteomes:UP000017948};
RN [1] {ECO:0000313|EMBL:CDE88125.1, ECO:0000313|Proteomes:UP000017948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:729 {ECO:0000313|Proteomes:UP000017948};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDE88125.1}.
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DR EMBL; CBJU010000022; CDE88125.1; -; Genomic_DNA.
DR AlphaFoldDB; R7LHH0; -.
DR Proteomes; UP000017948; 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:CDE88125.1};
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}; Transferase {ECO:0000256|HAMAP-Rule:MF_00165}.
FT DOMAIN 9..195
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 210 AA; 24009 MW; F1B53BBEA875BCEC CRC64;
MSNGMFITFE GADGCGKTTQ QMLAADYLES KGYEVLITRE PGAKGLGEDI RKILLDYKGP
VSERCESLLF LADRAQHVDN MILPAIEKGQ IVLCDRYTDS TVAYQGYGRQ QNLERIKKLN
DFATNLLKPD LTFVFNIDVE TSMQRVGKEK DRMESEGKEF HNRVRNGYLE IAKQEPERIK
VIDASMSIEE IHEEVKKVID FYLNYGKHSQ
//
