ID   KTHY_PYRAB              Reviewed;         205 AA.
AC   Q9V1E9; G8ZGI2;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Probable thymidylate kinase;
DE            EC=2.7.4.9;
DE   AltName: Full=dTMP kinase;
GN   Name=tmk; OrderedLocusNames=PYRAB04780; ORFNames=PAB0319;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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; AJ248284; CAB49400.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69861.1; -; Genomic_DNA.
DR   PIR; A75165; A75165.
DR   RefSeq; WP_010867602.1; NC_000868.1.
DR   AlphaFoldDB; Q9V1E9; -.
DR   SMR; Q9V1E9; -.
DR   STRING; 272844.PAB0319; -.
DR   EnsemblBacteria; CAB49400; CAB49400; PAB0319.
DR   GeneID; 1495374; -.
DR   KEGG; pab:PAB0319; -.
DR   PATRIC; fig|272844.11.peg.505; -.
DR   eggNOG; arCOG01891; Archaea.
DR   HOGENOM; CLU_049131_1_3_2; -.
DR   OMA; WIHEVIK; -.
DR   OrthoDB; 114844at2157; -.
DR   PhylomeDB; Q9V1E9; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide biosynthesis; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..205
FT                   /note="Probable thymidylate kinase"
FT                   /id="PRO_0000155392"
FT   BINDING         10..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   205 AA;  23513 MW;  1B011D41DEAC5115 CRC64;
     MRGYFVVLEG IDGSGKTTQA KLLAEWFEEQ GWDVLLTKEP TDTEFGRLIR ELVLKNSIID
     GSRISYEAEA LLFAADRAEH VKKVILPALE KGKVVICDRY LYSSLAYQWA RGLSLEWLMQ
     INSFAPRPDL AILLDLPVKE SIRRTKARGN MSEFDKLLEL QRKVRMNYLK LAEMFKEMRI
     VNAMASVEEV HEDIVALVKH ELLGL