ID A0A154R2N2_9GAMM Unreviewed; 210 AA.
AC A0A154R2N2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Thymidine kinase {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|HAMAP-Rule:MF_00124};
DE EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|HAMAP-Rule:MF_00124};
GN Name=tdk {ECO:0000256|HAMAP-Rule:MF_00124};
GN ORFNames=RhoFW510R10_14250 {ECO:0000313|EMBL:KZC32050.1};
OS Rhodanobacter sp. FW510-R10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1524462 {ECO:0000313|EMBL:KZC32050.1, ECO:0000313|Proteomes:UP000076310};
RN [1] {ECO:0000313|EMBL:KZC32050.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW510-R10 {ECO:0000313|EMBL:KZC32050.1};
RX PubMed=27048805; DOI=10.1128/mBio.02234-15;
RA Hemme C.L., Green S.J., Rishishwar L., Prakash O., Pettenato A.,
RA Chakraborty R., Deutschbauer A.M., Van Nostrand J.D., Wu L., He Z.,
RA Jordan I.K., Hazen T.C., Arkin A.P., Kostka J.E., Zhou J.;
RT "Lateral Gene Transfer in a Heavy Metal-Contaminated-Groundwater Microbial
RT Community.";
RL MBio 7:e02234-e02215(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00124,
CC ECO:0000256|RuleBase:RU000544};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00124}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00124}.
CC -!- SIMILARITY: Belongs to the thymidine kinase family.
CC {ECO:0000256|ARBA:ARBA00007587, ECO:0000256|HAMAP-Rule:MF_00124,
CC ECO:0000256|RuleBase:RU004165}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00124}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZC32050.1}.
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DR EMBL; LVJU01000023; KZC32050.1; -; Genomic_DNA.
DR RefSeq; WP_068092844.1; NZ_LVJU01000023.1.
DR AlphaFoldDB; A0A154R2N2; -.
DR OrthoDB; 9781579at2; -.
DR Proteomes; UP000076310; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00124; Thymidine_kinase; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001267; Thymidine_kinase.
DR PANTHER; PTHR11441; THYMIDINE KINASE; 1.
DR PANTHER; PTHR11441:SF0; THYMIDINE KINASE, CYTOSOLIC; 1.
DR Pfam; PF00265; TK; 1.
DR PIRSF; PIRSF035805; TK_cell; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00124}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00124};
KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634, ECO:0000256|HAMAP-
KW Rule:MF_00124};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00124};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00124};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00124}.
FT ACT_SITE 89
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124,
FT ECO:0000256|PIRSR:PIRSR035805-1"
FT BINDING 9..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT BINDING 88..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
SQ SEQUENCE 210 AA; 23375 MW; 06A2925EC433F655 CRC64;
MAKLYFYYSA MNAGKTTTLL QSAYNYHERG MRTLILTPAL DDRFGDGVVA SRIGLKANAR
RFAGDEDLFA LVEADIAANG PLHCVFVDEA QFLTKAQVWQ ASDVVDRLGI PVLAYGLRTD
FRGELFEGSR YLLAWADELE EIKTICHTGR KATMVVRVDE HGRVVTDGPQ VEIGGNERYV
SVSRAEFKKI SEGNGRIELQ QAVLPLGERE
//
