ID A0A1C4SLF8_9ACTN Unreviewed; 1052 AA.
AC A0A1C4SLF8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, 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=GA0115234_1094107 {ECO:0000313|EMBL:SCE47827.1};
OS Streptomyces sp. DvalAA-43.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1839762 {ECO:0000313|EMBL:SCE47827.1, ECO:0000313|Proteomes:UP000199186};
RN [1] {ECO:0000313|EMBL:SCE47827.1, ECO:0000313|Proteomes:UP000199186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DvalAA-43 {ECO:0000313|EMBL:SCE47827.1,
RC ECO:0000313|Proteomes:UP000199186};
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;
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}.
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DR EMBL; FMBW01000071; SCE47827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4SLF8; -.
DR OrthoDB; 9774907at2; -.
DR Proteomes; UP000199186; 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; 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};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:SCE47827.1};
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}; Transferase {ECO:0000256|HAMAP-Rule:MF_00165};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 43..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 322..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 379..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 421..444
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 512..695
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
FT REGION 262..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1016
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 514..521
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ SEQUENCE 1052 AA; 112463 MW; 469FE0ED9E1ACC79 CRC64;
MTRAEQPTVV SPTSDTLAAD SRERAVRALL RVPPLKRLWS AQLVGSTGDA LALLVLVLMS
LQAAVLEGSF GAGYRGAAFA VAAVFGARIL ATLLFGAVLL GPLTTLTAPG GPLDRRWLMI
GTDGLRLALL VVAPLWIDWM PDKALMMILI TVFVVGAAER LWTVAKDGAA PALLPGPPPE
GAAVRPLPDH LDALRRLSIR TDFAAIPVAA VVLLIATLVG NLLGSGLEWF SIHQAALGSY
VAAGLFSASI STLYFLELPG TQTPRPRSPL EGLRRPSAGG GPGKGRTGAV PLIVGASAAI
AGAIAAAAAV SVLHAADLGG GPATFALLIL ALTGGTGVGI RTAEKVLPTL SRRRLLALAT
AVTGIALLAM GLVPDTATVL MLTVLAGYAA GVAAHTGHVL VDQETEEFRR ARTTEHLQAV
VRVLIAVGAL AGPLLAAAIG AHRLGSGDFV FEHGGAAFAL MLIGALLLPV AVIVLAKTDD
RSGVPLRRDL REALRGGDPA VAPAATGFFI ALEGGDGAGK STQVEALAEW IRAKGHEVVV
TREPGATPVG KRLRSILLDV SSAGLSNRAE ALLYAADRAE HVDSVVRPAL ERGAIVISDR
YIDSSVAYQG AGRDLSPTEI ARISRWATSG LVPHLTVLLD VDPETARERF TEAPDRLESE
PPEFHARVRS GFLTLAAADP TRYLIVDAGQ DPESITTVVR HRLDRLLPLS EAEIKAQEEA
RKAAEEEARR KAEEEAARKA EEERLERERQ EQLAKLRAEE EERKARELEE ARRREAERQA
EEARQRAEEA RRVAEEERAR REAEEAAREA EQARLRRQAE EEARLRKEAE ALRLEKQRKA
EEALLRSEEA RRRAEAEAAA AAEKARAEAA AAASVPENEI TVPTPIVNPN DVTQQVPAPD
GSSSSTSSSS DEAETAMIPK IQDRSDRAGA ADETTVLPQV RDIRDANPAD RVPRGIFRDE
RPAGSAAESE NERTRELPQI DDPHAGAPRP AQNHWDGQEH QERPARRPRP DWAEETPLDD
LPTLADELLG DHRDQHDDGD PGRSGRGRRP RR
//
