GenomeNet

Database: UniProt
Entry: KTHY_CAMC5
LinkDB: KTHY_CAMC5
Original site: KTHY_CAMC5 
ID   KTHY_CAMC5              Reviewed;         194 AA.
AC   A7GYH0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   16-OCT-2019, entry version 66.
DE   RecName: Full=Thymidylate kinase {ECO:0000255|HAMAP-Rule:MF_00165};
DE            EC=2.7.4.9 {ECO:0000255|HAMAP-Rule:MF_00165};
DE   AltName: Full=dTMP kinase {ECO:0000255|HAMAP-Rule:MF_00165};
GN   Name=tmk {ECO:0000255|HAMAP-Rule:MF_00165};
GN   OrderedLocusNames=Ccur92_09580; ORFNames=CCV52592_1098;
OS   Campylobacter curvus (strain 525.92).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360105;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=525.92;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT   feces.";
RL   Submitted (JUL-2007) 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:0000255|HAMAP-
CC       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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00165};
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00165}.
DR   EMBL; CP000767; EAU00131.1; -; Genomic_DNA.
DR   RefSeq; WP_009650446.1; NC_009715.2.
DR   SMR; A7GYH0; -.
DR   PRIDE; A7GYH0; -.
DR   EnsemblBacteria; EAU00131; EAU00131; CCV52592_1098.
DR   KEGG; ccv:CCV52592_1098; -.
DR   eggNOG; ENOG4108ZMD; Bacteria.
DR   eggNOG; COG0125; LUCA.
DR   HOGENOM; HOG000229077; -.
DR   KO; K00943; -.
DR   OMA; GMAYSQF; -.
DR   OrthoDB; 1585072at2; -.
DR   BioCyc; CCUR360105:G1G9H-986-MONOMER; -.
DR   Proteomes; UP000006380; 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   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   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00041; DTMP_kinase; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Kinase; Nucleotide biosynthesis;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN         1    194       Thymidylate kinase.
FT                                /FTId=PRO_1000123563.
FT   NP_BIND       7     14       ATP. {ECO:0000255|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   194 AA;  21702 MW;  B9A357C076862C93 CRC64;
     MYVLFEGVDG VGKSTQIEMI ARAHEDSLVT KEPGGTKIGQ KLREILLGGD FKLSARAEIL
     LFLADRAEHY QKMIKPNSSR LILSDRGFVS GVAYALANDA SLKIDDLLWL NSFALEGKFA
     DKIVFFEASE TLIKKRLSSR GLIDAIEARG LKYLLKVQEC MKEVLKAHKF NVLYIDASED
     IATINAKIEN FIKF
//
DBGET integrated database retrieval system