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Database: UniProt
Entry: A0A143Y3F5_9FIRM
LinkDB: A0A143Y3F5_9FIRM
Original site: A0A143Y3F5_9FIRM 
ID   A0A143Y3F5_9FIRM        Unreviewed;       208 AA.
AC   A0A143Y3F5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   08-MAY-2019, entry version 15.
DE   RecName: Full=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   ECO:0000313|EMBL:CVI73735.1};
GN   ORFNames=BN3660_03294 {ECO:0000313|EMBL:CVI73735.1};
OS   Eubacteriaceae bacterium CHKCI004.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae.
OX   NCBI_TaxID=1780380 {ECO:0000313|EMBL:CVI73735.1, ECO:0000313|Proteomes:UP000199324};
RN   [1] {ECO:0000313|EMBL:CVI73735.1, ECO:0000313|Proteomes:UP000199324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHKC4 {ECO:0000313|EMBL:CVI73735.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC       salvage pathways of dTTP synthesis. {ECO:0000256|HAMAP-
CC       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:0000256|HAMAP-
CC         Rule:MF_00165, ECO:0000256|SAAS:SAAS01114966};
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000256|SAAS:SAAS01070220}.
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DR   EMBL; FCNR01000068; CVI73735.1; -; Genomic_DNA.
DR   Proteomes; UP000199324; Unassembled WGS sequence.
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   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 {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070209}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000199324};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:CVI73735.1};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070211};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070205};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199324};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204, ECO:0000313|EMBL:CVI73735.1}.
FT   DOMAIN        9    196       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND      10     17       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
FT   COILED      138    158       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   208 AA;  23080 MW;  E49D254E634A1534 CRC64;
     MKGIFIVMEG PDGSGKSTQI ALLKQYLDEV GCECLITREP GGTAIGEAVR NIILNPDHEE
     MSDVTEMLLY AASRAQLMSE VIIPALEAGK IVISDRFVDS SIVYQGIARG LGTDTVAAVN
     RPGIGQYEPD CIFFIDISEE EGIRRKKLQN KLDRMEQESI DFHSMVSRGY REVLSGREEV
     IHIDGSASVE HIQNQIREEL KKRIGKLS
//
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