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Database: UniProt
Entry: A0A1H4N875_9RHOB
LinkDB: A0A1H4N875_9RHOB
Original site: A0A1H4N875_9RHOB 
ID   A0A1H4N875_9RHOB        Unreviewed;       226 AA.
AC   A0A1H4N875;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   08-MAY-2019, entry version 7.
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=SAMN05519105_1573 {ECO:0000313|EMBL:SEB91499.1};
OS   Rhodobacter sp. 24-YEA-8.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1884310 {ECO:0000313|EMBL:SEB91499.1, ECO:0000313|Proteomes:UP000199640};
RN   [1] {ECO:0000313|EMBL:SEB91499.1, ECO:0000313|Proteomes:UP000199640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=24-YEA-8 {ECO:0000313|EMBL:SEB91499.1,
RC   ECO:0000313|Proteomes:UP000199640};
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; FNSK01000001; SEB91499.1; -; Genomic_DNA.
DR   Proteomes; UP000199640; 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:UP000199640};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:SEB91499.1};
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:UP000199640};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204}.
FT   DOMAIN       25    214       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND      27     34       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   226 AA;  24747 MW;  561EB5C83E400DB5 CRC64;
     MSGQRQWLRP LRPAEAELTG LFLSFEGIDG SGKSTQARRL AESLRAEGRK VTLTREPGGS
     PGAEEIRRLV LEGATDRWSA ETEILLFTAA RRDHVEKTIR PALARGEVVI CDRFADSTRI
     FQGLTRGDLT ATVDQLHDLM IGIEPDLTLL IDLAPETGLA RATARQGHEM RFEDMGLAFQ
     TAARDGFLTL AHAHPGRFRV ISGDASPDQI AARIRETVAP ELPPSS
//
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