ID A0A249L329_9ACTN Unreviewed; 672 AA.
AC A0A249L329;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=B1sIIB91_00095 {ECO:0000313|EMBL:ASY23345.1};
OS Candidatus Nanopelagicus abundans.
OC Bacteria; Actinomycetota; Actinomycetes; Candidatus Nanopelagicales;
OC Candidatus Nanopelagicaceae; Nanopelagicus.
OX NCBI_TaxID=1884916 {ECO:0000313|EMBL:ASY23345.1, ECO:0000313|Proteomes:UP000217210};
RN [1] {ECO:0000313|EMBL:ASY23345.1, ECO:0000313|Proteomes:UP000217210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-IIB-91 {ECO:0000313|EMBL:ASY23345.1};
RA Neuenschwander S.M., Salcher M., Ghai R., Pernthaler J.;
RT "High microdiversification within the ubiquitous acI lineage of
RT Actinobacteria.";
RL Submitted (JUL-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; CP016779; ASY23345.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A249L329; -.
DR KEGG; nab:B1sIIB91_00095; -.
DR OrthoDB; 9774907at2; -.
DR Proteomes; UP000217210; 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; 1.
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:ASY23345.1};
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:UP000217210};
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 61..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 372..396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..439
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
FT BINDING 472..479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ SEQUENCE 672 AA; 73020 MW; 8E83458AA7DE12C4 CRC64;
MSLPYPAAPA QSVSRNVLAI PAFRKLWQAM AFSSFGDWLG LLACTALAQQ LAGGDYAKAN
FAIAGVFIVR LLPAALLGPF AGVIADRFDR RRLMIICDIL RFSLYLSIPI VGNYFWLYTA
TILVEIVTLF WSPAKEASVP NLVPKLKLES ANQVSLLAAY GTAPIAAIVF STLAIFTGAI
NSALGNKTQA SAADLALYIN AISFAFCAYT IWRLKEIPEG PGKNLKQISL GKSLWDGFSF
IKDSKIIKGL IFGMLGAFFA AGAVIGLART FVDDLQAGEA AYGILFGSVF LGLALGISFG
PKVFSQFSRR RLFGISLTIS GILLVTLSLM LNLVLAIFIT IILGLFAGIS WVTGFTMLGL
EVEDEVRGRT FAFVQSLIRV ALVLVLAVSP LIAAAIGQHT YTFRTTTLTY NGAAFTMFFA
GLIAVLVGVI SYIQMRDRPN VSLLSDIKSA FRGELGTITG QATAGVFITF EGGEGSGKST
QTKLLKDWLE KNNETVLLTR EPGGTPLGNQ LRDILLDNKT GNISPRAEAL MYAADRANHV
YTMIRPALEK GEVVISDRFF DSSVAYQGAG RVLSPAEVAR ISRWATESLT PTLTIIMDLP
AEIGLARLQS TDRLESEPLA FHERVRHEYL NLAYQDPERF LLVDATLSIE QIHQVIIERV
GLIKALKRNQ KN
//
