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Database: UniProt
Entry: D4W2W4_9FIRM
LinkDB: D4W2W4_9FIRM
Original site: D4W2W4_9FIRM 
ID   D4W2W4_9FIRM            Unreviewed;       222 AA.
AC   D4W2W4;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   08-MAY-2019, entry version 41.
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:EFF64724.1};
GN   ORFNames=CUW_1617 {ECO:0000313|EMBL:EFF64724.1};
OS   Turicibacter sanguinis PC909.
OC   Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Turicibacter.
OX   NCBI_TaxID=702450 {ECO:0000313|EMBL:EFF64724.1, ECO:0000313|Proteomes:UP000002938};
RN   [1] {ECO:0000313|EMBL:EFF64724.1, ECO:0000313|Proteomes:UP000002938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC909 {ECO:0000313|EMBL:EFF64724.1,
RC   ECO:0000313|Proteomes:UP000002938};
RX   PubMed=21183674; DOI=10.1128/JB.01328-10;
RA   Cuiv P.O., Klaassens E.S., Durkin A.S., Harkins D.M., Foster L.,
RA   McCorrison J., Torralba M., Nelson K.E., Morrison M.;
RT   "Draft genome sequence of Turicibacter sanguinis PC909, isolated from
RT   human feces.";
RL   J. Bacteriol. 193:1288-1289(2011).
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:EFF64724.1}.
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DR   EMBL; ADMN01000023; EFF64724.1; -; Genomic_DNA.
DR   RefSeq; WP_006783714.1; NZ_ADMN01000023.1.
DR   STRING; 702450.CUW_1617; -.
DR   EnsemblBacteria; EFF64724; EFF64724; CUW_1617.
DR   eggNOG; ENOG4108ZMD; Bacteria.
DR   eggNOG; COG0125; LUCA.
DR   OrthoDB; 1585072at2; -.
DR   Proteomes; UP000002938; 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};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002938};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:EFF64724.1};
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:UP000002938};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204, ECO:0000313|EMBL:EFF64724.1}.
FT   DOMAIN       21    212       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND      23     30       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   222 AA;  24838 MW;  2AA402ECC2C2CA09 CRC64;
     MGFEIYLAKG VMMMSGFFIT LEGGEGAGKT TIANELIQKL SELGIETLYT REPGGIKIAE
     QIREVILDRE NTEMDSRTEA LLYAAARRQH LVEKVKPAMD AGKIVLCDRF VDSSIVYQGY
     ARGIGMDEVR EINQFAIEGF MPDMTIFFDI KPEDGLARIA ANSGREVNRL DLEGLEFHQL
     VYEGYKIQAN LFSERIVTVD ATQSIQAVTN EICQLILEKL GK
//
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