ID G0CAV1_XANCA Unreviewed; 209 AA.
AC G0CAV1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
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 ECO:0000313|EMBL:AEL09332.1};
GN ORFNames=XCR_4476 {ECO:0000313|EMBL:AEL09332.1};
OS Xanthomonas campestris pv. raphani 756C.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=990315 {ECO:0000313|EMBL:AEL09332.1, ECO:0000313|Proteomes:UP000001633};
RN [1] {ECO:0000313|EMBL:AEL09332.1, ECO:0000313|Proteomes:UP000001633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=756C {ECO:0000313|EMBL:AEL09332.1,
RC ECO:0000313|Proteomes:UP000001633};
RX PubMed=21784931; DOI=10.1128/JB.05262-11;
RA Bogdanove A.J., Koebnik R., Lu H., Furutani A., Angiuoli S.V., Patil P.B.,
RA Van Sluys M.A., Ryan R.P., Meyer D.F., Han S.W., Aparna G., Rajaram M.,
RA Delcher A.L., Phillippy A.M., Puiu D., Schatz M.C., Shumway M.,
RA Sommer D.D., Trapnell C., Benahmed F., Dimitrov G., Madupu R., Radune D.,
RA Sullivan S., Jha G., Ishihara H., Lee S.W., Pandey A., Sharma V.,
RA Sriariyanun M., Szurek B., Vera-Cruz C.M., Dorman K.S., Ronald P.C.,
RA Verdier V., Dow J.M., Sonti R.V., Tsuge S., Brendel V.P., Rabinowicz P.D.,
RA Leach J.E., White F.F., Salzberg S.L.;
RT "Two new complete genome sequences offer insight into host and tissue
RT specificity of plant pathogenic Xanthomonas spp.";
RL J. Bacteriol. 193:5450-5464(2011).
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}.
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DR EMBL; CP002789; AEL09332.1; -; Genomic_DNA.
DR RefSeq; WP_012439677.1; NC_017271.1.
DR AlphaFoldDB; G0CAV1; -.
DR GeneID; 58015460; -.
DR KEGG; xcp:XCR_4476; -.
DR PATRIC; fig|990315.4.peg.4211; -.
DR HOGENOM; CLU_064400_2_1_6; -.
DR Proteomes; UP000001633; Chromosome.
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 209 AA; 23340 MW; 3625FF0E7EF79074 CRC64;
MAKLYFYYSA MNAGKTTTLL QSAHNYRERG MRTSILTPKL DHRAGSGVVA SRIGLRADGQ
TFDRQTELLQ LIERDIAAHG PLHCVLVDEA QFLSRAQVWQ LSEVVDRLRI PVLCYGLRTD
FRGELFEGSQ FLLAWADELE EIKTICHSGS KATMTVRVDA QGHAVQDGPQ VEIGGNERYV
SVSRAEFKKI MRGEGRIDPL QIALPLPPA
//
