ID A0A1V0ACN7_9ACTN Unreviewed; 680 AA.
AC A0A1V0ACN7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=BKM31_46840 {ECO:0000313|EMBL:AQZ67984.1};
OS Nonomuraea sp. ATCC 55076.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=1909395 {ECO:0000313|EMBL:AQZ67984.1, ECO:0000313|Proteomes:UP000190797};
RN [1] {ECO:0000313|Proteomes:UP000190797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55076 {ECO:0000313|Proteomes:UP000190797};
RX PubMed=28626548; DOI=10.1039/c6md00637j;
RA Nazari B., Forneris C.C., Gibson M.I., Moon K., Schramma K.R.,
RA Seyedsayamdost M.R.;
RT "Nonomuraea sp. ATCC 55076 harbours the largest actinomycete chromosome to
RT date and the kistamicin biosynthetic gene cluster.";
RL Med. Chem. Commun. 8:780-788(2017).
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; CP017717; AQZ67984.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0ACN7; -.
DR STRING; 1909395.BKM31_46840; -.
DR KEGG; noa:BKM31_46840; -.
DR OrthoDB; 9774907at2; -.
DR Proteomes; UP000190797; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
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; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00165; Thymidylate_kinase; 1.
DR InterPro; IPR020846; MFS_dom.
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; PS50850; MFS; 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:AQZ67984.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, 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:UP000190797};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00165};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 407..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..433
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
FT REGION 661..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 467..474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ SEQUENCE 680 AA; 72572 MW; 14DCF52722DF2A2A CRC64;
MTAPGRSRPT HVLANAPFRR LWTAMSVCSL GDWLNLLALT ALAGNLTQGD YRVQSLAVGG
VFVAKMLPAV LLGPLAGVFA DRFDRRLTMF CADLARFAVV LSIPFVDNYQ WVIIATVLVE
CVNLFWVPAK EATVPNLVPK AQLEQANQLN LLVTYGTAPV AAMLFAALSV AGDLIAGIVP
FPLGRDATGL ALVVNACAYL VSAFLIFTLR DIPKRDGAIS TPSVLKQVVE GWRFVGGNRL
VRGLVIGMLG AFAAGGAVVG VAKVYVEALG GGDAAYGVVF GAVFVGMALG MFFGLRLLRE
LSRRRLFGLA ITVAGVVLVA IALVHNLVIV VMLTVVLGAC AGIAWIIGYT LIGLEVEDAL
RGRTFSFLQS TARVTLLLVV SLANPLAALF GLHTLGLGEF SYRFDGTNLV LVIGGALAVG
VGLLALRQMD DRKGVSLAAD LLAAVRGERF PTEAAEHVPG LFIAFEGGEG SGKTTQSRMI
AIWMRDQGYD VVQTREPGST KVGMRLRAIL LDAAERGLSA RSEALLYAAD RAEHVEKVIR
PALYRGSIVI TDRYVDSSLA YQGAGRALDP ADVSKINAWA TGGLVPHLTV LIDTPPEVGL
TRLGGAADRI ESEPMEFHER VRKEFRALAA SAPERYLVVD GTLPQDVVTR QIQDRIREIL
PDPVPRESED ATGTMPAIRD
//
