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Database: UniProt
Entry: G7VCA7_9CREN
LinkDB: G7VCA7_9CREN
Original site: G7VCA7_9CREN 
ID   G7VCA7_9CREN            Unreviewed;       199 AA.
AC   G7VCA7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Probable thymidylate kinase {ECO:0000256|HAMAP-Rule:MF_00165};
DE            EC=2.7.4.9 {ECO:0000256|HAMAP-Rule:MF_00165};
DE   AltName: Full=dTMP kinase {ECO:0000256|HAMAP-Rule:MF_00165};
GN   Name=tmk {ECO:0000256|HAMAP-Rule:MF_00165};
GN   ORFNames=P186_2407 {ECO:0000313|EMBL:AET33793.1};
OS   Pyrobaculum ferrireducens.
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=1104324 {ECO:0000313|EMBL:AET33793.1, ECO:0000313|Proteomes:UP000005867};
RN   [1] {ECO:0000313|EMBL:AET33793.1, ECO:0000313|Proteomes:UP000005867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1860 {ECO:0000313|EMBL:AET33793.1,
RC   ECO:0000313|Proteomes:UP000005867};
RX   PubMed=22247528; DOI=10.1128/JB.06465-11;
RA   Mardanov A.V., Gumerov V.M., Slobodkina G.B., Beletsky A.V.,
RA   Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT   "Complete genome sequence of strain 1860, a crenarchaeon of the genus
RT   pyrobaculum able to grow with various electron acceptors.";
RL   J. Bacteriol. 194:727-728(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         Evidence={ECO:0000256|ARBA:ARBA00001008, ECO:0000256|HAMAP-
CC         Rule:MF_00165};
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00009776, ECO:0000256|HAMAP-Rule:MF_00165}.
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DR   EMBL; CP003098; AET33793.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7VCA7; -.
DR   STRING; 1104324.P186_2407; -.
DR   KEGG; pyr:P186_2407; -.
DR   eggNOG; arCOG01891; Archaea.
DR   HOGENOM; CLU_049131_0_2_2; -.
DR   OrthoDB; 43083at2157; -.
DR   Proteomes; UP000005867; 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   CDD; cd01672; TMPK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00041; DTMP_kinase; 1.
DR   PANTHER; PTHR10344; THYMIDYLATE KINASE; 1.
DR   PANTHER; PTHR10344:SF4; UMP-CMP KINASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:AET33793.1};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165}.
FT   DOMAIN          6..180
FT                   /note="Thymidylate kinase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02223"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ   SEQUENCE   199 AA;  22268 MW;  DB252970160455C2 CRC64;
     MAFVAVEGID GSGKSTVIQL LAKLLPKVYV TKEPSDGPVG RLIKEWALKG GSVDPHVDAL
     LFAADRIEHY KREVEPKIRE GYLVISERYV ESSIAYQGAA GVPIDFIKYI NKLVPRPDLT
     VILDVDPEVA EARIRRRGHV EKYEYVQFLR RVREIYLTRA AEEGHPVVDA SRSPEEVAAD
     VAEIIHRSVI EPRGRQSLG
//
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