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Database: UniProt
Entry: A0A1H8FU67_9BURK
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ID   A0A1H8FU67_9BURK        Unreviewed;       214 AA.
AC   A0A1H8FU67;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   08-MAY-2019, entry version 8.
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   ORFNames=SAMN02745977_01187 {ECO:0000313|EMBL:SEN35256.1};
OS   Brachymonas denitrificans DSM 15123.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Brachymonas.
OX   NCBI_TaxID=1121117 {ECO:0000313|EMBL:SEN35256.1, ECO:0000313|Proteomes:UP000199531};
RN   [1] {ECO:0000313|EMBL:SEN35256.1, ECO:0000313|Proteomes:UP000199531}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15123 {ECO:0000313|EMBL:SEN35256.1,
RC   ECO:0000313|Proteomes:UP000199531};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FOCW01000001; SEN35256.1; -; Genomic_DNA.
DR   BioCyc; GCF_900110225:BMW28_RS05930-MONOMER; -.
DR   Proteomes; UP000199531; 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; IPR018094; Thymidylate_kinase.
DR   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00041; DTMP_kinase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070209};
KW   Complete proteome {ECO:0000313|Proteomes:UP000199531};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:SEN35256.1};
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:UP000199531};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204}.
FT   DOMAIN       12    202       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND      14     21       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   214 AA;  23452 MW;  6944D0289BA8792F CRC64;
     MNPSGQGLFI SFEGIDGAGK TTHIGTLAET FARQGRTVLR TREPGGTALA EKLRSLVLHD
     PMGALTEALL VFAARCDHVQ QVIAPALARG EVVLCDRFAD ATFAYQGAGR DFDWGTLRAL
     EAMVLRQEDG TQLQPDLTLW FDVSPAIAAQ RLADARQPDK FEAESTGFFE RVAGGYARRM
     RESPARFGRI DASRTPQEVW QQVEAVMAQK GWLA
//
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