ID C0BLS9_9BACT Unreviewed; 228 AA.
AC C0BLS9;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 13-SEP-2023, entry version 63.
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=Flav3CDRAFT_1190 {ECO:0000313|EMBL:EEG43712.1};
OS Flavobacteria bacterium MS024-3C.
OC Bacteria; Bacteroidota; Flavobacteriia.
OX NCBI_TaxID=487797 {ECO:0000313|EMBL:EEG43712.1, ECO:0000313|Proteomes:UP000003631};
RN [1] {ECO:0000313|EMBL:EEG43712.1, ECO:0000313|Proteomes:UP000003631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS024-3C {ECO:0000313|EMBL:EEG43712.1,
RC ECO:0000313|Proteomes:UP000003631};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Woyke T., Xie G., Copeland A., Gonzalez J., Han C., Kiss H., Saw J.,
RA Senin P., Chatterji S., Cheng J.-F., Eisen J.A., Sieracki M.E.,
RA Stepanauskas R.;
RT "Assembling the metagenome, one cell at a time.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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:EEG43712.1}.
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DR EMBL; ABVW01000001; EEG43712.1; -; Genomic_DNA.
DR AlphaFoldDB; C0BLS9; -.
DR STRING; 487797.Flav3CDRAFT_1190; -.
DR OrthoDB; 9781579at2; -.
DR Proteomes; UP000003631; 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; 3.30.60.20; -; 1.
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 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}; Reference proteome {ECO:0000313|Proteomes:UP000003631};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00124}.
FT REGION 206..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT BINDING 21..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT BINDING 93..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
SQ SEQUENCE 228 AA; 25602 MW; 07B6EA10F7E3D26D CRC64;
MFLENTVNHE EPFGWIEVIC GSMFSGKTEE LIRRLKRAQF AKQRIEIFKP QIDTRYHDEM
VVSHDENQIR STPVPAAANI RILADQCDVV GIDEAQFFDA EIIHVCNDLA NKGKRVIVAG
LDMDFKGNPF GPMPALMATA EYVTKVHAVC TRTGNLANYS FRKSANEKLV LLGETTEYEP
LSRSAYFKAM LKERVKDLEV NDPIALADPS KTAGNLNPIP DTKQKQSN
//
