KTHY_PSEAE
ID KTHY_PSEAE Reviewed; 210 AA.
AC Q9HZN8;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Thymidylate kinase;
DE EC=2.7.4.9;
DE AltName: Full=dTMP kinase;
GN Name=tmk; OrderedLocusNames=PA2962;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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}.
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DR EMBL; AE004091; AAG06350.1; -; Genomic_DNA.
DR PIR; E83275; E83275.
DR RefSeq; NP_251652.1; NC_002516.2.
DR RefSeq; WP_003091125.1; NZ_QZGE01000009.1.
DR PDB; 3UWK; X-ray; 1.91 A; A/B=1-210.
DR PDB; 3UWO; X-ray; 1.70 A; A/B=1-210.
DR PDB; 3UXM; X-ray; 1.95 A; A/B/C/D=2-210.
DR PDB; 4E5U; X-ray; 1.81 A; A/B=1-210.
DR PDB; 4EDH; X-ray; 1.32 A; A/B=1-210.
DR PDB; 4ESH; X-ray; 1.95 A; A=1-210.
DR PDB; 4GMD; X-ray; 1.98 A; A/B/C/D=1-210.
DR PDBsum; 3UWK; -.
DR PDBsum; 3UWO; -.
DR PDBsum; 3UXM; -.
DR PDBsum; 4E5U; -.
DR PDBsum; 4EDH; -.
DR PDBsum; 4ESH; -.
DR PDBsum; 4GMD; -.
DR AlphaFoldDB; Q9HZN8; -.
DR SMR; Q9HZN8; -.
DR STRING; 287.DR97_4977; -.
DR PaxDb; Q9HZN8; -.
DR PRIDE; Q9HZN8; -.
DR DNASU; 878730; -.
DR EnsemblBacteria; AAG06350; AAG06350; PA2962.
DR GeneID; 878730; -.
DR KEGG; pae:PA2962; -.
DR PATRIC; fig|208964.12.peg.3108; -.
DR PseudoCAP; PA2962; -.
DR HOGENOM; CLU_049131_0_2_6; -.
DR InParanoid; Q9HZN8; -.
DR OMA; VMTREPG; -.
DR PhylomeDB; Q9HZN8; -.
DR BioCyc; PAER208964:G1FZ6-3014-MON; -.
DR BRENDA; 2.7.4.9; 5087.
DR Proteomes; UP000002438; 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; IPR018094; Thymidylate_kinase.
DR Pfam; PF02223; Thymidylate_kin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00041; DTMP_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..210
FT /note="Thymidylate kinase"
FT /id="PRO_0000155324"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:4EDH"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3UWK"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:4EDH"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:4EDH"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:4EDH"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:4EDH"
FT HELIX 63..80
FT /evidence="ECO:0007829|PDB:4EDH"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:4EDH"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:4EDH"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:4EDH"
FT TURN 105..109
FT /evidence="ECO:0007829|PDB:4EDH"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:4EDH"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:4EDH"
FT HELIX 139..146
FT /evidence="ECO:0007829|PDB:4EDH"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:4EDH"
FT HELIX 160..176
FT /evidence="ECO:0007829|PDB:4EDH"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:4EDH"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:4EDH"
FT HELIX 190..208
FT /evidence="ECO:0007829|PDB:4EDH"
SQ SEQUENCE 210 AA; 23109 MW; 49B40C96F8ED338E CRC64;
MTGLFVTLEG PEGAGKSTNR DYLAERLRER GIEVQLTREP GGTPLAERIR ELLLAPSDEP
MAADTELLLM FAARAQHLAG VIRPALARGA VVLCDRFTDA TYAYQGGGRG LPEARIAALE
SFVQGDLRPD LTLVFDLPVE IGLARAAARG RLDRFEQEDR RFFEAVRQTY LQRAAQAPER
YQVLDAGLPL AEVQAGLDRL LPNLLERLNG
