ID A0A317MSL1_9ACTN Unreviewed; 256 AA.
AC A0A317MSL1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=BDW27_102120 {ECO:0000313|EMBL:PWV57255.1};
OS Nocardiopsis sp. L17-MgMaSL7.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=1938893 {ECO:0000313|EMBL:PWV57255.1, ECO:0000313|Proteomes:UP000246681};
RN [1] {ECO:0000313|EMBL:PWV57255.1, ECO:0000313|Proteomes:UP000246681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L17-MgMaSL7 {ECO:0000313|EMBL:PWV57255.1,
RC ECO:0000313|Proteomes:UP000246681};
RA Partida-Martinez L.;
RT "The Agave Microbiome: Exploring the role of microbial communities in plant
RT adaptations to desert environments.";
RL Submitted (MAY-2018) 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 -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC {ECO:0000256|HAMAP-Rule:MF_00165}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:PWV57255.1}.
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DR EMBL; QGTF01000002; PWV57255.1; -; Genomic_DNA.
DR RefSeq; WP_017545488.1; NZ_QGTF01000002.1.
DR AlphaFoldDB; A0A317MSL1; -.
DR Proteomes; UP000246681; Unassembled WGS sequence.
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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00165; Thymidylate_kinase; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039430; Thymidylate_kin-like_dom.
DR InterPro; IPR018094; Thymidylate_kinase.
DR Pfam; PF02223; Thymidylate_kin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:PWV57255.1};
KW Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00165}.
FT DOMAIN 19..206
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
SQ SEQUENCE 256 AA; 27941 MW; 54BAB0C598CB8DAE CRC64;
MRNTAVHPAC TRGPLISAEG VNGVGKTYLT NRAVEALREP PLMLDEFSER VHGRHGLGED
LLDALREASG RDPFLRGGTP MAEALLLMAM KRHDLDTVLP DLAAGRSVVE GRSVDTTAVY
QALLLCPDDP EGALDTARAL LDLAASYRCL PDLTVLVTDD AAQAVERAQR RDRRILTPEQ
SGFLVAACEL YERLAATDPA RYRVVDRRRV DEFEAAELIR SWILDAGADL GCVREPWQDP
QTPCLCCGQG VEPVPA
//
