KTHY_AQUAE
ID KTHY_AQUAE Reviewed; 195 AA.
AC O67099;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Thymidylate kinase;
DE EC=2.7.4.9;
DE AltName: Full=dTMP kinase;
GN Name=tmk; OrderedLocusNames=aq_969;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC salvage pathways of dTTP synthesis. {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000657; AAC07063.1; -; Genomic_DNA.
DR PIR; H70383; H70383.
DR RefSeq; NP_213662.1; NC_000918.1.
DR RefSeq; WP_010880600.1; NC_000918.1.
DR PDB; 2PBR; X-ray; 1.96 A; A/B=1-195.
DR PDB; 4S2E; X-ray; 2.35 A; A/B=1-195.
DR PDB; 4S35; X-ray; 1.55 A; A/B=1-195.
DR PDB; 5H56; X-ray; 1.70 A; A/B=1-195.
DR PDB; 5H5B; X-ray; 2.05 A; A/B=1-195.
DR PDB; 5H5K; X-ray; 2.30 A; A/B=1-195.
DR PDB; 5XAI; X-ray; 2.00 A; A/B=1-195.
DR PDB; 5XB2; X-ray; 2.16 A; A/B=1-195.
DR PDB; 5XB3; X-ray; 1.77 A; A/B=1-195.
DR PDB; 5XB5; X-ray; 2.23 A; A/B=1-195.
DR PDB; 5XBH; X-ray; 2.23 A; A/B=1-195.
DR PDBsum; 2PBR; -.
DR PDBsum; 4S2E; -.
DR PDBsum; 4S35; -.
DR PDBsum; 5H56; -.
DR PDBsum; 5H5B; -.
DR PDBsum; 5H5K; -.
DR PDBsum; 5XAI; -.
DR PDBsum; 5XB2; -.
DR PDBsum; 5XB3; -.
DR PDBsum; 5XB5; -.
DR PDBsum; 5XBH; -.
DR AlphaFoldDB; O67099; -.
DR SMR; O67099; -.
DR STRING; 224324.aq_969; -.
DR EnsemblBacteria; AAC07063; AAC07063; aq_969.
DR KEGG; aae:aq_969; -.
DR PATRIC; fig|224324.8.peg.762; -.
DR eggNOG; COG0125; Bacteria.
DR HOGENOM; CLU_049131_0_2_0; -.
DR InParanoid; O67099; -.
DR OMA; VMTREPG; -.
DR OrthoDB; 1585072at2; -.
DR EvolutionaryTrace; O67099; -.
DR Proteomes; UP000000798; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide biosynthesis;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..195
FT /note="Thymidylate kinase"
FT /id="PRO_0000155230"
FT BINDING 7..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:4S35"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:4S35"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:4S35"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:4S35"
FT HELIX 57..74
FT /evidence="ECO:0007829|PDB:4S35"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:4S35"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:4S35"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:4S35"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:4S35"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:4S35"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:4S35"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:4S35"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:5H56"
FT HELIX 149..165
FT /evidence="ECO:0007829|PDB:4S35"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:4S35"
FT HELIX 178..189
FT /evidence="ECO:0007829|PDB:4S35"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:4S35"
SQ SEQUENCE 195 AA; 22370 MW; F3C2A94D4930956E CRC64;
MLIAFEGIDG SGKTTQAKKL YEYLKQKGYF VSLYREPGGT KVGEVLREIL LTEELDERTE
LLLFEASRSK LIEEKIIPDL KRDKVVILDR FVLSTIAYQG YGKGLDVEFI KNLNEFATRG
VKPDITLLLD IPVDIALRRL KEKNRFENKE FLEKVRKGFL ELAKEEENVV VIDASGEEEE
VFKEILRALS GVLRV