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Database: UniProt/TrEMBL
Entry: H2FQC7_CORPS
LinkDB: H2FQC7_CORPS
Original site: H2FQC7_CORPS 
ID   H2FQC7_CORPS            Unreviewed;       206 AA.
AC   H2FQC7;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   16-APR-2014, entry version 15.
DE   RecName: Full=Thymidylate kinase;
DE            EC=2.7.4.9;
DE   AltName: Full=dTMP kinase;
GN   Name=tmk; ORFNames=Cp3995_0522;
OS   Corynebacterium pseudotuberculosis 3/99-5.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1087452;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=3/99-5;
RX   PubMed=22887652; DOI=10.1128/JB.00918-12;
RA   Pethick F.E., Lainson A.F., Yaga R., Flockhart A., Smith D.G.,
RA   Donachie W., Cerdeira L.T., Silva A., Bol E., Lopes T.S.,
RA   Barbosa M.S., Pinto A.C., Dos Santos A.R., Soares S.C., Almeida S.S.,
RA   Guimaraes L.C., Aburjaile F.F., Abreu V.A., Ribeiro D., Fiaux K.K.,
RA   Diniz C.A., Barbosa E.G., Pereira U.P., Hassan S.S., Ali A.,
RA   Bakhtiar S.M., Dorella F.A., Carneiro A.R., Ramos R.T., Rocha F.S.,
RA   Schneider M.P., Miyoshi A., Azevedo V., Fontaine M.C.;
RT   "Complete Genome Sequences of Corynebacterium pseudotuberculosis
RT   Strains 3/99-5 and 42/02-A, Isolated from Sheep in Scotland and
RT   Australia, Respectively.";
RL   J. Bacteriol. 194:4736-4737(2012).
CC   -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC       salvage pathways of dTTP synthesis (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + dTMP = ADP + dTDP.
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
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DR   EMBL; CP003152; AEX38991.1; -; Genomic_DNA.
DR   RefSeq; YP_005122640.1; NC_016781.1.
DR   EnsemblBacteria; AEX38991; AEX38991; Cp3995_0522.
DR   GeneID; 11675592; -.
DR   KEGG; cpl:Cp3995_0522; -.
DR   KO; K00943; -.
DR   BioCyc; CPSE1087452:GJTM-538-MONOMER; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00165; Thymidylate_kinase; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR018095; Thymidylate_kin_CS.
DR   InterPro; IPR018094; Thymidylate_kinase.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Kinase; Nucleotide biosynthesis;
KW   Nucleotide-binding; Transferase.
SQ   SEQUENCE   206 AA;  23068 MW;  B8A9588B2C77D947 CRC64;
     MIIAIEGIDG AGKNTLVRAL VEKLDARVLG FPRYQDSIHA HLAQKALYQE MGDVSDSIYA
     MALLFALDRR EIAEELRSYK GSEDVILLDR YVSSNAAYSA ARAQDWNLVA WVSHLEFEEF
     GLPTPDIQVL LNTSPEVAAQ RAAKREEQDQ DRSRDCYETD SSLQVRTSDA YARLAEEKRF
     SPWIVAQPGD SVDDVALKII QTLGTM
//
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