ID Q2IES5_ANADE Unreviewed; 561 AA.
AC Q2IES5;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
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 OrderedLocusNames=Adeh_3313 {ECO:0000313|EMBL:ABC83080.1};
OS Anaeromyxobacter dehalogenans (strain 2CP-C).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC83080.1, ECO:0000313|Proteomes:UP000001935};
RN [1] {ECO:0000313|Proteomes:UP000001935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA Zhulin I.B., Loeffler F.E., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL Submitted (JAN-2006) 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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00165};
CC -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC {ECO:0000256|HAMAP-Rule:MF_00165}.
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DR EMBL; CP000251; ABC83080.1; -; Genomic_DNA.
DR RefSeq; WP_011422362.1; NC_007760.1.
DR AlphaFoldDB; Q2IES5; -.
DR STRING; 290397.Adeh_3313; -.
DR KEGG; ade:Adeh_3313; -.
DR eggNOG; COG0125; Bacteria.
DR HOGENOM; CLU_477201_0_0_7; -.
DR OrthoDB; 9774907at2; -.
DR Proteomes; UP000001935; Chromosome.
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; IPR018094; Thymidylate_kinase.
DR Pfam; PF02223; Thymidylate_kin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00165};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:ABC83080.1};
KW Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165};
KW Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:ABC83080.1}.
FT DOMAIN 5..149
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
FT REGION 213..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..234
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 7..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ SEQUENCE 561 AA; 57895 MW; 74F5E1A83C530A64 CRC64;
MLVSFEGIDG SGKTALSNLV CERLRRGGRE VVHARERGVL ATAAARRVRE LTRDPRLLEL
SPRAELCLNL AREAQQLEEV VRPALARGAL CVADRSLHSI LALAVAGRGL PRAEVEAAVR
AASGGTWPDL AVLVDVDPDL ARLRKRVGKI LEGRADEPGS RKGLAGHGLQ VRVREHLAAE
AAAAPASWLR VANEGRALEA LADEVADAIA ARAAGGRAPR RPPAPAPRSA RPPAPAGPAG
IAARFEAAVD ALAAREPALA AHLLAGIPGR AAHARRTALA GRCPAVVARA LEGLSDPESH
ALRWALAGRA PADVAAGLGA DASPEAMRLR AALLARAPGP AVAGLVAADG ADAWALRAEA
LERGELEGVL RGLAGLGTER AWALRADGIG RGLWEAVGRS LAGVDGARAD AMRSALAAHD
RLAALRGTAG VESGPARALR ERLFPLAPKR VLRTLAGNAA PWTWALRERA LAFTKEALDA
VDGMDHPRAW ALRAEGVARW PAAAVSSLRH LAATAPGREI VAAALRAAPA SLPVLRNAHA
VLALAAPAPG LPAAVEESCT P
//
