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Database: UniProt
Entry: G0AXG2_9GAMM
LinkDB: G0AXG2_9GAMM
Original site: G0AXG2_9GAMM 
ID   G0AXG2_9GAMM            Unreviewed;       208 AA.
AC   G0AXG2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Thymidylate kinase {ECO:0000256|ARBA:ARBA00017144, ECO:0000256|HAMAP-Rule:MF_00165};
DE            EC=2.7.4.9 {ECO:0000256|ARBA:ARBA00012980, ECO:0000256|HAMAP-Rule:MF_00165};
DE   AltName: Full=dTMP kinase {ECO:0000256|ARBA:ARBA00029962, ECO:0000256|HAMAP-Rule:MF_00165};
GN   Name=tmk {ECO:0000256|HAMAP-Rule:MF_00165};
GN   ORFNames=Sbal175_1919 {ECO:0000313|EMBL:AEG11189.1};
OS   Shewanella baltica BA175.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=693974 {ECO:0000313|EMBL:AEG11189.1, ECO:0000313|Proteomes:UP000002249};
RN   [1] {ECO:0000313|EMBL:AEG11189.1, ECO:0000313|Proteomes:UP000002249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BA175 {ECO:0000313|EMBL:AEG11189.1,
RC   ECO:0000313|Proteomes:UP000002249};
RX   PubMed=22328742; DOI=10.1128/JB.06468-11;
RA   Caro-Quintero A., Auchtung J., Deng J., Brettar I., Hofle M., Tiedje J.M.,
RA   Konstantinidis K.T.;
RT   "Genome sequencing of five Shewanella baltica strains recovered from the
RT   oxic-anoxic interface of the Baltic Sea.";
RL   J. Bacteriol. 194:1236-1236(2012).
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; CP002767; AEG11189.1; -; Genomic_DNA.
DR   RefSeq; WP_006081922.1; NC_017571.1.
DR   AlphaFoldDB; G0AXG2; -.
DR   GeneID; 11774813; -.
DR   KEGG; sbb:Sbal175_1919; -.
DR   HOGENOM; CLU_049131_0_1_6; -.
DR   Proteomes; UP000002249; 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; IPR018095; Thymidylate_kin_CS.
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.
DR   PROSITE; PS01331; THYMIDYLATE_KINASE; 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:AEG11189.1};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00165};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:AEG11189.1}.
FT   DOMAIN          10..199
FT                   /note="Thymidylate kinase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02223"
FT   BINDING         12..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ   SEQUENCE   208 AA;  22603 MW;  95B29FCC9D62886B CRC64;
     MSVFAKFIVI EGLEGAGKSS AINLIRDFIE KHTGKAPICT REPGGTPLAE RIRDLVKIAD
     ATDPLCDEAE CLLIYAARAQ LVANVIKPAL AQGQWVLGDR HNLSSLAYQG GGRGLMPLVE
     AVSTATLKGF KPDLTLYLDL DPKLGLTRAA KRGELDRIEQ QAIDFFERAR ATYLKLASED
     DSIVVIDASQ TMAEVHKDIL AVLQAMAW
//
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