KTHY_STAAM
ID KTHY_STAAM Reviewed; 205 AA.
AC P65248; Q99WC1;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=SAV0482;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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; BA000017; BAB56644.1; -; Genomic_DNA.
DR RefSeq; WP_001272126.1; NC_002758.2.
DR PDB; 2CCG; X-ray; 2.30 A; A/B=1-205.
DR PDB; 2CCJ; X-ray; 1.70 A; A/B=1-205.
DR PDB; 2CCK; X-ray; 2.21 A; A/B=1-205.
DR PDB; 4DWJ; X-ray; 2.74 A; A/B/C/D/E/F/G/H=1-205.
DR PDB; 4EAQ; X-ray; 1.85 A; A/B=1-205.
DR PDB; 4F4I; X-ray; 2.45 A; A/B=1-205.
DR PDB; 4GFD; X-ray; 1.80 A; A/B=1-205.
DR PDB; 4MQB; X-ray; 1.55 A; A/B=1-205.
DR PDBsum; 2CCG; -.
DR PDBsum; 2CCJ; -.
DR PDBsum; 2CCK; -.
DR PDBsum; 4DWJ; -.
DR PDBsum; 4EAQ; -.
DR PDBsum; 4F4I; -.
DR PDBsum; 4GFD; -.
DR PDBsum; 4MQB; -.
DR AlphaFoldDB; P65248; -.
DR SMR; P65248; -.
DR PaxDb; P65248; -.
DR EnsemblBacteria; BAB56644; BAB56644; SAV0482.
DR KEGG; sav:SAV0482; -.
DR HOGENOM; CLU_049131_0_2_9; -.
DR OMA; VMTREPG; -.
DR PhylomeDB; P65248; -.
DR BioCyc; SAUR158878:SAV_RS02640-MON; -.
DR EvolutionaryTrace; P65248; -.
DR PRO; PR:P65248; -.
DR Proteomes; UP000002481; 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 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; Transferase.
FT CHAIN 1..205
FT /note="Thymidylate kinase"
FT /id="PRO_0000155339"
FT BINDING 9..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00165"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:4MQB"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:4MQB"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:4MQB"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:4MQB"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:4MQB"
FT HELIX 42..53
FT /evidence="ECO:0007829|PDB:4MQB"
FT HELIX 59..76
FT /evidence="ECO:0007829|PDB:4MQB"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:4MQB"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:4MQB"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:4MQB"
FT TURN 101..105
FT /evidence="ECO:0007829|PDB:4MQB"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:4MQB"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:4MQB"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:4MQB"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4DWJ"
FT HELIX 154..171
FT /evidence="ECO:0007829|PDB:4MQB"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:4EAQ"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:4MQB"
FT HELIX 187..203
FT /evidence="ECO:0007829|PDB:4MQB"
SQ SEQUENCE 205 AA; 23425 MW; 71F9C96511FF3A5E CRC64;
MSAFITFEGP EGSGKTTVIN EVYHRLVKDY DVIMTREPGG VPTGEEIRKI VLEGNDMDIR
TEAMLFAASR REHLVLKVIP ALKEGKVVLC DRYIDSSLAY QGYARGIGVE EVRALNEFAI
NGLYPDLTIY LNVSAEVGRE RIIKNSRDQN RLDQEDLKFH EKVIEGYQEI IHNESQRFKS
VNADQPLENV VEDTYQTIIK YLEKI
