ID A0A1A9BJF8_9ACTN Unreviewed; 718 AA.
AC A0A1A9BJF8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=GA0070622_6332 {ECO:0000313|EMBL:SBT69211.1};
OS Micromonospora sediminicola.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=946078 {ECO:0000313|EMBL:SBT69211.1, ECO:0000313|Proteomes:UP000199558};
RN [1] {ECO:0000313|EMBL:SBT69211.1, ECO:0000313|Proteomes:UP000199558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45794 {ECO:0000313|EMBL:SBT69211.1,
RC ECO:0000313|Proteomes:UP000199558};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC {ECO:0000256|HAMAP-Rule:MF_00165}.
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DR EMBL; FLRH01000004; SBT69211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A9BJF8; -.
DR STRING; 946078.GA0070622_6332; -.
DR Proteomes; UP000199558; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd06173; MFS_MefA_like; 1.
DR CDD; cd01672; TMPK; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00165; Thymidylate_kinase; 1.
DR InterPro; IPR036259; MFS_trans_sf.
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 InterPro; IPR010290; TM_effector.
DR NCBIfam; TIGR00041; DTMP_kinase; 1.
DR PANTHER; PTHR43266; MACROLIDE-EFFLUX PROTEIN; 1.
DR PANTHER; PTHR43266:SF5; MFS DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF05977; MFS_3; 1.
DR Pfam; PF02223; Thymidylate_kin; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 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|HAMAP-Rule:MF_00165};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:SBT69211.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00165};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 93..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 324..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 483..672
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
FT REGION 690..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 485..492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ SEQUENCE 718 AA; 75365 MW; 0EABAD45C44169EA CRC64;
MSSPGTQADR SGIAAIRSVL RIRPFRRLWI VLSAASFGDW LGLLATALFA ASQVSGSTAQ
GAAFGGVTAI RLLPALVLGP VAGVFADRFD RRWTMVICDL LRFVLFASIP LYALTGAAGG
LVVGWALIAT FLIESITLMW IPAKEAAVPN LIPRTRLEAA NQLTLITTYG LTPVAAAVAL
AVLDRGVRGA VGGDLPDWAE PAQLALWFNA FSRLATALVV AFGIKEISEA QRGEGERAEQ
SMFRQFAEGW KFIGQTPLVR GLVLGIFGAF AGGGIVVGTA KFFANSLGAG DAAFSLLFGA
IFVGLALGIG LGPMIVRDMS RRRWFGMSIV LASASVLVLA FAIHLSMAIV GAILVGAGAG
MAFLAGTTLL GGEVADEVRG RVFAVVQIGT RLVLILAIAL SSLLVGVGGS RQLTIADLGI
SISSTRLLLL AAGAAGIFAG ISAFGQMDDK KGVPVLADLW GSIRGRPLMP AEPFVSSGLF
VVFEGGEGAG KSTQLAALAE RLRGQGRDVV VTREPGATGV GERIRSLVLG TTHDDAPSPR
AEALLYAADR AHHVATVVRP ALVRGAVVVS DRYVDSSLAY QGAGRTLPVD EVSWLSSWAT
GGLKPDLVVL LDVDPRTGLG RVESRNEGAD RLEAESLAFH ERVRYAFLDL AAGDPKRYLV
LDASRPVEEI ADAVARRVDE FLVDPAAIVH PRPAQGPDTS VQPELSDAEL VTMEQTRR
//
