ID   H6L8E0_SAPGL            Unreviewed;       184 AA.
AC   H6L8E0;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Thymidine kinase {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|RuleBase:RU000544};
DE            EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|RuleBase:RU000544};
GN   Name=tdk {ECO:0000313|EMBL:AFC26504.1};
GN   OrderedLocusNames=SGRA_3788 {ECO:0000313|EMBL:AFC26504.1};
OS   Saprospira grandis (strain Lewin).
OC   Bacteria; Bacteroidota; Saprospiria; Saprospirales; Saprospiraceae;
OC   Saprospira.
OX   NCBI_TaxID=984262 {ECO:0000313|EMBL:AFC26504.1, ECO:0000313|Proteomes:UP000007519};
RN   [1] {ECO:0000313|EMBL:AFC26504.1, ECO:0000313|Proteomes:UP000007519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lewin {ECO:0000313|EMBL:AFC26504.1,
RC   ECO:0000313|Proteomes:UP000007519};
RX   PubMed=22675601; DOI=10.4056/sigs.2445005;
RA   Saw J.H., Yuryev A., Kanbe M., Hou S., Young A.G., Aizawa S., Alam M.;
RT   "Complete genome sequencing and analysis of Saprospira grandis str. Lewin,
RT   a predatory marine bacterium.";
RL   Stand. Genomic Sci. 6:84-93(2012).
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|RuleBase:RU000544};
CC   -!- SIMILARITY: Belongs to the thymidine kinase family.
CC       {ECO:0000256|ARBA:ARBA00007587, ECO:0000256|RuleBase:RU004165}.
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DR   EMBL; CP002831; AFC26504.1; -; Genomic_DNA.
DR   RefSeq; WP_015694091.1; NC_016940.1.
DR   AlphaFoldDB; H6L8E0; -.
DR   STRING; 984262.SGRA_3788; -.
DR   KEGG; sgn:SGRA_3788; -.
DR   eggNOG; COG1435; Bacteria.
DR   HOGENOM; CLU_064400_3_1_10; -.
DR   OrthoDB; 9781579at2; -.
DR   Proteomes; UP000007519; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-EC.
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   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|RuleBase:RU000544};
KW   DNA synthesis {ECO:0000256|ARBA:ARBA00022634,
KW   ECO:0000256|RuleBase:RU000544};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000544};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000544};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007519};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000544}.
FT   ACT_SITE        85
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR035805-1"
SQ   SEQUENCE   184 AA;  20952 MW;  7E1C6D82DF5C0043 CRC64;
     MNGKLHLILG PMFSGKSTLL LTRYRRYRIA GKACLLVKYA KDCRYDDSAA MIVTHDKLRY
     EATACTKLAE LDDLVQDYDV ICIDEIQFYP DAADFADRWA NQGKIVECCG LSGDYKREPF
     EQISRLIPRC DDITHVKAVC KSSGLDAPFS QRFSQEEEQE VIGGSDKYQA VSRAVYLQQQ
     KKED
//