UniProt: F5L9X0

Database: UniProt
Entry: F5L9X0_CALTT

LinkDB:  F5L9X0_CALTT 
Original site:  F5L9X0_CALTT

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (4)   
   InterPro (3)   
   Pfam (1)   
Literature (2)   
   PubMed (2)   
All databases (16)   

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ID   F5L9X0_CALTT            Unreviewed;       214 AA.
AC   F5L9X0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
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:QZT34329.1};
GN   ORFNames=CathTA2_2625 {ECO:0000313|EMBL:EGL81840.1}, HUR95_02675
GN   {ECO:0000313|EMBL:QZT34329.1};
OS   Caldalkalibacillus thermarum (strain TA2.A1).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldalkalibacillus.
OX   NCBI_TaxID=986075 {ECO:0000313|EMBL:EGL81840.1, ECO:0000313|Proteomes:UP000010716};
RN   [1] {ECO:0000313|EMBL:EGL81840.1, ECO:0000313|Proteomes:UP000010716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TA2.A1 {ECO:0000313|EMBL:EGL81840.1,
RC   ECO:0000313|Proteomes:UP000010716};
RX   PubMed=21685297; DOI=10.1128/JB.05035-11;
RA   Kalamorz F., Keis S., McMillan D.G., Olsson K., Stanton J.A., Stockwell P.,
RA   Black M.A., Klingeman D.M., Land M.L., Han C.S., Martin S.L., Becher S.A.,
RA   Peddie C.J., Morgan H.W., Matthies D., Preiss L., Meier T., Brown S.D.,
RA   Cook G.M.;
RT   "Draft genome sequence of the thermoalkaliphilic Caldalkalibacillus
RT   thermarum strain TA2.A1.";
RL   J. Bacteriol. 193:4290-4291(2011).
RN   [2] {ECO:0000313|EMBL:QZT34329.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TA2.A1 {ECO:0000313|EMBL:QZT34329.1};
RX   PubMed=33030592;
RA   de Jong S.I., van den Broek M.A., Merkel A.Y., de la Torre Cortes P.,
RA   Kalamorz F., Cook G.M., van Loosdrecht M.C.M., McMillan D.G.G.;
RT   "Genomic analysis of Caldalkalibacillus thermarum TA2.A1 reveals aerobic
RT   alkaliphilic metabolism and evolutionary hallmarks linking alkaliphilic
RT   bacteria and plant life.";
RL   Extremophiles 24:923-935(2020).
RN   [3] {ECO:0000313|EMBL:QZT34329.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TA2.A1 {ECO:0000313|EMBL:QZT34329.1};
RA   de Jong S., van den Broek M., Merkel A., de la Torre Cortes P.,
RA   Kalamorz F., Cook G., van Loosdrecht M., McMillan D.;
RL   Submitted (AUG-2021) 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-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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001008, ECO:0000256|HAMAP-
CC         Rule:MF_00165};
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00009776, ECO:0000256|HAMAP-Rule:MF_00165}.
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DR   EMBL; AFCE01000160; EGL81840.1; -; Genomic_DNA.
DR   EMBL; CP082237; QZT34329.1; -; Genomic_DNA.
DR   RefSeq; WP_007506022.1; NZ_CP082237.1.
DR   AlphaFoldDB; F5L9X0; -.
DR   KEGG; cthu:HUR95_02675; -.
DR   eggNOG; COG0125; Bacteria.
DR   OrthoDB; 9774907at2; -.
DR   Proteomes; UP000010716; Unassembled WGS sequence.
DR   Proteomes; UP000825179; Chromosome.
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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01672; TMPK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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   NCBIfam; TIGR00041; DTMP_kinase; 1.
DR   PANTHER; PTHR10344; THYMIDYLATE KINASE; 1.
DR   PANTHER; PTHR10344:SF4; THYMIDYLATE KINASE; 1.
DR   Pfam; PF02223; Thymidylate_kin; 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_00165};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:EGL81840.1};
KW   Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727, ECO:0000256|HAMAP-
KW   Rule:MF_00165};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00165}; Reference proteome {ECO:0000313|Proteomes:UP000010716};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:QZT34329.1}.
FT   DOMAIN          8..202
FT                   /note="Thymidylate kinase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02223"
FT   BINDING         10..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ   SEQUENCE   214 AA;  24043 MW;  301DED6789DF9FE1 CRC64;
     MAGLFITFEG PDGAGKTTQL TLLAEALKAS GYDVTVTREP GGTLISDRIR RIILDPDHQS
     MRAQTEVLLY AASRAQHVLE KIKPALAQGK IVLCDRFVDA SIAYQGYGLG VGEEQVRMIN
     QFATQGLVPH KTFLLDIAAE EGRRRLAERK QAEFKQGLDR IEQKDLAYHE RVRRGFLRLA
     EQEDRIVLID ASQPVEVIHQ QILREVRSLL QQKA
//

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