ID A0A0N1FGV1_9ACTN Unreviewed; 1107 AA.
AC A0A0N1FGV1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=OK006_1585 {ECO:0000313|EMBL:KPH96883.1};
OS Actinobacteria bacterium OK006.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPH96883.1, ECO:0000313|Proteomes:UP000037912};
RN [1] {ECO:0000313|EMBL:KPH96883.1, ECO:0000313|Proteomes:UP000037912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK006 {ECO:0000313|EMBL:KPH96883.1,
RC ECO:0000313|Proteomes:UP000037912};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four Actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (SEP-2015) 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;
CC Evidence={ECO:0000256|ARBA:ARBA00001008, ECO:0000256|HAMAP-
CC Rule:MF_00165};
CC -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC {ECO:0000256|ARBA:ARBA00009776, ECO:0000256|HAMAP-Rule:MF_00165}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPH96883.1}.
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DR EMBL; LJCU01000291; KPH96883.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1FGV1; -.
DR PATRIC; fig|1592326.3.peg.11338; -.
DR Proteomes; UP000037912; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 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 NCBIfam; TIGR00041; DTMP_kinase; 1.
DR PANTHER; PTHR10344; THYMIDYLATE KINASE; 1.
DR PANTHER; PTHR10344:SF4; THYMIDYLATE KINASE; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00165}; Hydrolase {ECO:0000313|EMBL:KPH96883.1};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:KPH96883.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00165};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:KPH96883.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 42..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 452..477
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 514..698
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
FT REGION 759..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1051
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 516..523
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ SEQUENCE 1107 AA; 116738 MW; 4BFCEA58AA6D2A77 CRC64;
MTRAEQPTAH TPAPDDALVA DSRERAVRAL LRRPQLKRLW SAHLVGGVGD ALALLVLVIL
VLQAAIAEGS FGGGYRGVAL AVAAVFGARV LATLLFGAVL LGPLTSLTSQ EGPLDRRWTM
VGADGLRAVL MLIAPLWIDW TPDNALAALL VLAFVTGVAE RFWTVCRESA APALLPAPPL
EGATVRPLPD HLDALRRLSL RTAFAAVPIA AVTLVVVSLV SNLLGAGIAW FDQHQGALAS
YVAAGLFAAS LSVLTSLELP DTRTPRARSP LEGLRRPRTG TGVDNGRTGA IPLLVLACAA
VAAAIAAAVA VSVLQAKDMG GGPVTYGLLV LALTGGVVIG IRTAPSVLPP LSRRRLLSLA
IAFTGIALLA AGLVPDVTTV LLIAGLAGIG AGVAANTGHA LLDQETEEYR RARTTEHLHA
VVRVSVALGA LLAPVVAAAI GPHRLENGKF VFAHGGAAFT LMLVGALLLP VAALVLAKVD
DRSGVPLRHD LLDALRGGDD PVQKSTANGF FIALEGGDGA GKSTQAEALA EWIRAKGHEV
VVTREPGATP VGKRLRSILL DVSSAGLSHR AEALLYAADR AEHVDTVVRP ALERGAVVIS
DRYIDSSVAY QGAGRDLSPT EIARINRWAT NGLVPHLTVL LDVSPEAARE RFTEAPDRLE
SEPVEFHTRV RSGFLTLAAA DPGRYLVVDA AQEPEAVTTV LRHRLDVMLP LSEAEVKAQE
EARKAAEEEA RRKAEEEAAR KAEEERLERE RQEQLARLRA EEEERKQREL EEAQRREAER
QAEEARQRAE EARRRAEEER ARLLAQEQAQ AAEQDRLRRL AEEQARLRAE AEERRLEKQR
KAEEALLRAE EARRAATDRA AAAAAAATAA STSASASASA STAASASSVT SAPASGSAPA
GSAEPAATGP VADNETTVPT PVVTPPSTSG GSVDETTVLR PVRSGESRQG SRSDSEETAK
LPKPPVPEEA AEKTAVLPPV VPGAADETAV LPPVAPGAAD ETAVLPPVRD GGAGAAPDAG
TGDPANRVPP GFFRDERAEP RPEKAGDRTR ELPQVNAEGA PRRRPRSDWA EETPLDDLPT
LADELLGPRD DDEQDDGREG RGGRRRR
//
