ID A0A101SNW2_9ACTN Unreviewed; 1107 AA.
AC A0A101SNW2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-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=AQJ66_33930 {ECO:0000313|EMBL:KUN77422.1};
OS Streptomyces bungoensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285568 {ECO:0000313|EMBL:KUN77422.1, ECO:0000313|Proteomes:UP000053024};
RN [1] {ECO:0000313|EMBL:KUN77422.1, ECO:0000313|Proteomes:UP000053024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41781 {ECO:0000313|EMBL:KUN77422.1,
RC ECO:0000313|Proteomes:UP000053024};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces bungoensis DSM 41781, type strain
RT for the species Streptomyces bungoensis.";
RL Submitted (OCT-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:KUN77422.1}.
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DR EMBL; LMWX01000064; KUN77422.1; -; Genomic_DNA.
DR RefSeq; WP_061929850.1; NZ_KQ948876.1.
DR AlphaFoldDB; A0A101SNW2; -.
DR STRING; 285568.AQJ66_33930; -.
DR OrthoDB; 9774907at2; -.
DR Proteomes; UP000053024; 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:KUN77422.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000053024};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00165};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 363..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 387..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 459..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 521..706
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..882
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..961
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 523..530
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ SEQUENCE 1107 AA; 117867 MW; 5413DF486F7460A5 CRC64;
MTRAEQPTAA HTPETPPAAE PDDALIADSR ERAVRSLLQR PQLRRLWSAQ LVSGVGDTLA
LLVLVLLVLQ TSIAEGSFGG GYRGVAFAVA TVFAARILAT LLFGAVLLGP LTALTAHGGP
LDRRWTMVGA DGVRAALLIV APLWIDWTPD DALALLLVTT FLTGVAERLW TVCRESAAPA
LLPAPPPEGA TVRPLPDHID ALRRLALRTS FLAIPLAAAA LVVAALLNNL LGTGVAWFDQ
HKAALAAYVA AGLFAASLSV LVYLELPGTP TPRARSPLEG LRRPRTGAGV DKGRTGAIPL
LVPACAAVAG AISTAVAVCV LHAKDLGGGP VLYGLLVLGL TGGVAVGIRT AHSVLPSLSR
RRLLALAIAF TGIALLAAGL VPDVTTVLLL VTLAGVSAGV AANTGHALLD QETEEYRRAR
TTEHLHAVVR VFIALGALIA PLVAALIGPH RLENGRFVFA HGGAAFTLML VGALLLPVAA
LVLAKVDDRS GVPLRQDLKD ALLGGDDPAT APAANGFFIA LEGGDGAGKS TQAEALAEWI
RAKGHEVVLT REPGATPVGK RLRSILLDVS SAGLSHRAEA LLYAADRAEH VDTVVRPALE
RGAVVISDRY IDSSVAYQGA GRDLSPTEVA RINRWATHGL VPHLTVLLDV SPETARERFT
EAPDRLESEP AEFHARVRAG FLTLAASDPG RYLVVDAGQE PEAVTTVIRH RLDTVLPLSE
AEVKAQEEAR KKAEEEARRK AEEEAARKVE EERLERERQE QLARLRAEEE ERKRRELEEA
QRREAERQAE EARQRAAEAA RRAEEERQRL IAEEKARAEE EARRKAEEER RRRQAEEEAR
LRADEEARQA RLRAEEEARR LEAQRKAEEA LLRAEEARRQ AAEAAAAADA AALRPSAPRP
AVPGGTPEQT GAGAGTKAVP PGADETVPTP VVSPDAEETA VLRGVREKLA GDKRKARSVP
DNEVTAELPQ PPVPSGAADE TAVLPPVPSG PADETAVLPP VTPGAADETA VLPPVRGASA
ADRVPAGFFR DERPAQDPDG EDRTREMPQL DADGTPRRRP RPDWAEETPL DDLPTLADEL
LGSHDEGQYG EPGEDQGRRG RGRGRRG
//
