ID F7T8S0_9BURK Unreviewed; 207 AA.
AC F7T8S0;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 08-MAY-2019, entry version 36.
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:EGP43319.1};
GN ORFNames=AXXA_26830 {ECO:0000313|EMBL:EGP43319.1};
OS Achromobacter insuavis AXX-A.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=1003200 {ECO:0000313|EMBL:EGP43319.1, ECO:0000313|Proteomes:UP000004853};
RN [1] {ECO:0000313|EMBL:EGP43319.1, ECO:0000313|Proteomes:UP000004853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AXX-A {ECO:0000313|EMBL:EGP43319.1,
RC ECO:0000313|Proteomes:UP000004853};
RA Bador J., Amoureux L., Neuwirth C.;
RL Submitted (JUN-2011) 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:EGP43319.1}.
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DR EMBL; AFRQ01000125; EGP43319.1; -; Genomic_DNA.
DR RefSeq; WP_006395336.1; NZ_GL982453.1.
DR STRING; 1003200.AXXA_26830; -.
DR EnsemblBacteria; EGP43319; EGP43319; AXXA_26830.
DR PATRIC; fig|1003200.3.peg.5309; -.
DR eggNOG; ENOG4108ZMD; Bacteria.
DR eggNOG; COG0125; LUCA.
DR Proteomes; UP000004853; 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:UP000004853};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:EGP43319.1};
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, ECO:0000313|EMBL:EGP43319.1}.
FT DOMAIN 10 193 Thymidylate_kin. {ECO:0000259|Pfam:
FT PF02223}.
FT NP_BIND 12 19 ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ SEQUENCE 207 AA; 22866 MW; BD1D9D2301779385 CRC64;
MTSRRRFITL EGVDGAGKST HTEWIAEFLR GQGLEVVSTR EPGGTPLGEK LRALVLTDPM
GLDTETLLMF AARCEHLHQV IEPTLARGAW VVCDRYTDAT YAYQGGGRGL GAARVAALET
WMQAGRPDRT WLFDVPLAVA RARLADAREP DRFEREGAAF FERTRAAYQA RAAAEPDRIQ
VIDSTRAIPE IRAELEAGLR QLVAARS
//
