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Database: UniProt
Entry: A0A1C3CWS9_9GAMM
LinkDB: A0A1C3CWS9_9GAMM
Original site: A0A1C3CWS9_9GAMM 
ID   A0A1C3CWS9_9GAMM        Unreviewed;       198 AA.
AC   A0A1C3CWS9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   08-MAY-2019, entry version 14.
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=BBP83_06980 {ECO:0000313|EMBL:ODA13180.1};
OS   Acinetobacter celticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=1891224 {ECO:0000313|EMBL:ODA13180.1, ECO:0000313|Proteomes:UP000186553};
RN   [1] {ECO:0000313|EMBL:ODA13180.1, ECO:0000313|Proteomes:UP000186553}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANC 4603 {ECO:0000313|EMBL:ODA13180.1,
RC   ECO:0000313|Proteomes:UP000186553};
RA   Radolfova-Krizova L., Nemec A.;
RT   "Acinetobacter sp. ANC 4603.";
RL   Submitted (JUL-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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ODA13180.1}.
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DR   EMBL; MBDL01000009; ODA13180.1; -; Genomic_DNA.
DR   RefSeq; WP_068887257.1; NZ_MBDL01000009.1.
DR   Proteomes; UP000186553; 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:UP000186553};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:ODA13180.1};
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   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204}.
FT   DOMAIN        5    193       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND       7     14       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   198 AA;  22499 MW;  3E357D1620815AEA CRC64;
     MFISFEGTEG VGKTTLIRKI YDHFIAQGQD VVLTREPGGT PMAEQIRALL LSVNHEEKMC
     NDTELLLMYA ARAQHLSQVI LPALEAGKTV LCDRFTDASF AYQCAGRGLS EDKLLLLNAN
     FVSRMPDFTF WLDAPIEIGM NRARARGELD RFEQEKVTFF EKVRAGYETL SVRHPERVKR
     LDASQSPEQV FEQALTYF
//
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