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Database: UniProt
Entry: X5EQK0_NEIME
LinkDB: X5EQK0_NEIME
Original site: X5EQK0_NEIME 
ID   X5EQK0_NEIME            Unreviewed;       206 AA.
AC   X5EQK0;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 54.
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   ECO:0000313|EMBL:AHW75274.1};
GN   ORFNames=I7J91_07715 {ECO:0000313|EMBL:MBH5540286.1}, I7L15_05140
GN   {ECO:0000313|EMBL:MBH2211358.1}, NMA510612_0973
GN   {ECO:0000313|EMBL:AHW75274.1};
OS   Neisseria meningitidis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=487 {ECO:0000313|EMBL:AHW75274.1, ECO:0000313|Proteomes:UP000023582};
RN   [1] {ECO:0000313|EMBL:AHW75274.1, ECO:0000313|Proteomes:UP000023582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=510612 {ECO:0000313|EMBL:AHW75274.1}, and NMA510612
RC   {ECO:0000313|Proteomes:UP000023582};
RX   PubMed=24812217;
RA   Zhang Y., Yang J., Xu L., Zhu Y., Liu B., Shao Z., Zhang X., Jin Q.;
RT   "Complete Genome Sequence of Neisseria meningitidis Serogroup A Strain
RT   NMA510612, Isolated from a Patient with Bacterial Meningitis in China.";
RL   Genome Announc. 2:e00360-14(2014).
RN   [2] {ECO:0000313|Proteomes:UP000023582}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NMA510612 {ECO:0000313|Proteomes:UP000023582};
RA   Zhang X., Zhang Y., Yang J., Zhu Y., Jin Q.;
RT   "Complete Genome Sequence of Neisseria meningitides, serogroup A strain
RT   510612.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:MBH2211358.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M43341 {ECO:0000313|EMBL:MBH5540286.1}, and OL22400
RC   {ECO:0000313|EMBL:MBH2211358.1};
RA   Topaz N., Kristiansen P.A., Schmink S., Congo-Ouedraogo M., Kambire D.,
RA   Mbaeyi S., Paye M., Sanou M., Sangare L., Ouedraogo R., Wang X.;
RT   "Molecular insights into meningococcal carriage isolates from Burkina Faso
RT   seven years after introduction of a serogroup A meningococcal conjugate
RT   vaccine.";
RL   Submitted (NOV-2020) 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; CP007524; AHW75274.1; -; Genomic_DNA.
DR   EMBL; JADXLT010000008; MBH2211358.1; -; Genomic_DNA.
DR   EMBL; JADYPM010000026; MBH5540286.1; -; Genomic_DNA.
DR   RefSeq; WP_002214191.1; NZ_QSWK01000074.1.
DR   KEGG; nmx:NMA510612_0973; -.
DR   PATRIC; fig|487.1203.peg.127; -.
DR   OMA; FLYTADH; -.
DR   Proteomes; UP000023582; Chromosome.
DR   Proteomes; UP000596799; Unassembled WGS sequence.
DR   Proteomes; UP000598179; Unassembled WGS sequence.
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; UMP-CMP KINASE 2, MITOCHONDRIAL; 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|HAMAP-Rule:MF_00165};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:AHW75274.1};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000313|EMBL:MBH2211358.1}.
FT   DOMAIN          8..196
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   206 AA;  23028 MW;  FC36374225FFDF5D CRC64;
     MKPQFITLDG IDGAGKSTNL AVIKAWFERR GLPVLFTREP GGTPVGEALR EILLNPETKA
     GLRAETLMMF AARMQHIEDV ILPALSDGIH VVSDRFTDAT FAYQGGGRGM PSEDIEILEH
     WVQGGLRPDL TLLLDVPLEV SMARIGQTRE KDRFEQEQAD FFMRVRSVYL NRAAACPERY
     AVIDSNLGLD EVRNSIEKVL DRHFGC
//
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