ID A0A1C5H412_9ACTN Unreviewed; 807 AA.
AC A0A1C5H412;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=GA0074704_1024 {ECO:0000313|EMBL:SCG40760.1};
OS Micromonospora siamensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=299152 {ECO:0000313|EMBL:SCG40760.1, ECO:0000313|Proteomes:UP000198210};
RN [1] {ECO:0000313|EMBL:SCG40760.1, ECO:0000313|Proteomes:UP000198210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45097 {ECO:0000313|EMBL:SCG40760.1,
RC ECO:0000313|Proteomes:UP000198210};
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; LT607751; SCG40760.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C5H412; -.
DR Proteomes; UP000198210; Chromosome i.
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:SCG40760.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000198210};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00165};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 118..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 351..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 414..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 439..460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 472..497
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 517..535
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 573..760
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 575..582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ SEQUENCE 807 AA; 83590 MW; 998310401BAFB695 CRC64;
MPNVGPARGG TAIESQQNGE SSGVSPTGPQ PGAHGPQPGA ADLGPDGPGP AHVARDRRAD
GADRRPAAPA DPAGASADPA ATPGAQRDAD SGPAGSPADR SGAAAIRSVL RIRPFRRLWI
VLGAASFGDW LGLLATSVFA AGQVQGSTAK GAAFGTTIAI RLLPALVLGP LAGVFADRFD
RRWTMVICDL LRFVLFASIP LYALTGAAGG LVVGWALIAT FLIESVTLLW IPAKEAAVPN
LIPRARLEAA NQLTLITTYG LTPVAAAIGL AVLDRGVRGA VGGDLPAWAE PAQLALWLNA
FSRLATALVV AFGIKEISHA QRGEGERAEQ SMFRQFADGW KYIGQTPLVR GLVLGIFGAF
AGGGIVIGTA KFFAASLGAG DAAFYMLFGA IFIGLALGIG LGPMIVREMS RRRWFGMSIV
LASASVMVLA FAIHLSMAIL GAILVGAGAG MAFLAGTTLL GGEVADEVRG RVFAVVQIGT
RLVLILAIAL SSLLVGVGGS RQLTIADLGI SVSSTRLLLL AAGAAGIFAG ISAFGQMDDK
KGVPVLADLW GSIRGRPLMP AEPFVSAGLF VVFEGGEGAG KSTQLAALAA RLRGQGRDVV
VTREPGATDV GAKIRSLVLE KSAPDAPSPR AEALLYAADR AHHVATVVRP ALIRGAVVVS
DRYVDSSLAY QGAGRTLPVD EVSWLSSWAT GGLKPDLVVL LDVDPRTGLS RVESRNEGTD
RLEAESVAFH ERVRYAFLDL AANDPKRYLV LDASRPAEEI AGLVARRVEE FLADPAGIVH
PRPAQGPDTS VQPELSDAEL VTLEHRT
//