ID A0A0M4TY62_9NOSO Unreviewed; 209 AA.
AC A0A0M4TY62;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=ACX27_19275 {ECO:0000313|EMBL:ALF54501.1};
OS Nostoc piscinale CENA21.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=224013 {ECO:0000313|EMBL:ALF54501.1, ECO:0000313|Proteomes:UP000062645};
RN [1] {ECO:0000313|Proteomes:UP000062645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CENA21 {ECO:0000313|Proteomes:UP000062645};
RA Leao T.F., Leao P.N., Guimaraes P.I., de Melo A.G.C., Ramos R.T.J.,
RA Silva A., Fiore M.F., Schneider M.P.C.;
RT "Genome Of Nitrogen-Fixing Cyanobacterium Nostoc piscinale CENA21 From
RT Solimoes/Amazon River Floodplain Sediments And Comparative Genomics To
RT Uncover Biosynthetic Natural Products Potential.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALF54501.1, ECO:0000313|Proteomes:UP000062645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CENA21 {ECO:0000313|EMBL:ALF54501.1,
RC ECO:0000313|Proteomes:UP000062645};
RX PubMed=27034496;
RA Leao T., Guimaraes P.I., de Melo A.G., Ramos R.T., Leao P.N., Silva A.,
RA Fiore M.F., Schneider M.P.;
RT "Draft Genome Sequence of the N2-Fixing Cyanobacterium Nostoc piscinale
RT CENA21, Isolated from the Brazilian Amazon Floodplain.";
RL Genome Announc. 4:0-0(2016).
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; CP012036; ALF54501.1; -; Genomic_DNA.
DR RefSeq; WP_062295032.1; NZ_CP012036.1.
DR AlphaFoldDB; A0A0M4TY62; -.
DR STRING; 224013.ACX27_19275; -.
DR PATRIC; fig|224013.5.peg.4605; -.
DR OrthoDB; 9774907at2; -.
DR Proteomes; UP000062645; Chromosome.
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; 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; 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; 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:ALF54501.1};
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}.
FT DOMAIN 8..199
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ SEQUENCE 209 AA; 23172 MW; 7900CAD162CA5C37 CRC64;
MSGKLIVFEG VEGCGKTTQM QLCCQWLESL GISVIVTREP GGTELGIHLR RLLLEKSEDK
PVADVTELLL YAADRAQHVE QELKPNLAAG KYILCDRYID STVAYQGYGR GLNMSLIEKL
NDIATSGLTS DLTIWLDVDV EVGFSRKRGD AAGLDRIEQE TIAFHRRVQQ GYSQLAAAHP
SRIVRVDGSL SKETVSSLIQ EILRQRLQV
//
