KTHY_GLOVI
ID KTHY_GLOVI Reviewed; 212 AA.
AC Q7NMT7;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Thymidylate kinase {ECO:0000255|HAMAP-Rule:MF_00165};
DE EC=2.7.4.9 {ECO:0000255|HAMAP-Rule:MF_00165};
DE AltName: Full=dTMP kinase {ECO:0000255|HAMAP-Rule:MF_00165};
GN Name=tmk {ECO:0000255|HAMAP-Rule:MF_00165}; OrderedLocusNames=glr0678;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
CC -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC salvage pathways of dTTP synthesis. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_00165};
CC -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00165}.
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DR EMBL; BA000045; BAC88619.1; -; Genomic_DNA.
DR RefSeq; NP_923624.1; NC_005125.1.
DR RefSeq; WP_011140680.1; NC_005125.1.
DR AlphaFoldDB; Q7NMT7; -.
DR SMR; Q7NMT7; -.
DR STRING; 251221.35211240; -.
DR EnsemblBacteria; BAC88619; BAC88619; BAC88619.
DR KEGG; gvi:glr0678; -.
DR PATRIC; fig|251221.4.peg.687; -.
DR eggNOG; COG0125; Bacteria.
DR HOGENOM; CLU_049131_0_0_3; -.
DR InParanoid; Q7NMT7; -.
DR OMA; VMTREPG; -.
DR OrthoDB; 1585072at2; -.
DR PhylomeDB; Q7NMT7; -.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004798; F:thymidylate kinase activity; IBA:GO_Central.
DR GO; GO:0009041; F:uridylate kinase activity; IBA:GO_Central.
DR GO; GO:0006233; P:dTDP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006235; P:dTTP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006227; P:dUDP biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF02223; Thymidylate_kin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide biosynthesis; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..212
FT /note="Thymidylate kinase"
FT /id="PRO_0000155279"
FT BINDING 7..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00165"
SQ SEQUENCE 212 AA; 23112 MW; 9311D2E81840D388 CRC64;
MFITFEGGEG CGKTTQLTLL GDWLEKRCHR VVRTREPGGT ALGRSLRGLL LDARSEITPT
AELLLYATDR AEHLARVVRP ALASGAAVLC DRFSDSTVAY QGYGRGLDLG LIERLNAIAT
GGLLPDLTFW LKLDPQAGLV RRLASNGNTP DRIEAETLAF HQRVHMGFAA LANRYPGRIR
PVDAGLSVEA TAEQIRSAVD VFLNENQSKL EK
