ID A0A0R2CAI1_9LACO Unreviewed; 213 AA.
AC A0A0R2CAI1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 08-MAY-2019, entry version 18.
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 ORFNames=FD21_GL000754 {ECO:0000313|EMBL:KRM88817.1};
OS Lactobacillus vini DSM 20605.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1133569 {ECO:0000313|EMBL:KRM88817.1, ECO:0000313|Proteomes:UP000051576};
RN [1] {ECO:0000313|EMBL:KRM88817.1, ECO:0000313|Proteomes:UP000051576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20605 {ECO:0000313|EMBL:KRM88817.1,
RC ECO:0000313|Proteomes:UP000051576};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O.,
RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E.,
RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R.,
RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through
RT comparative genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC salvage pathways of dTTP synthesis. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_00165, ECO:0000256|SAAS:SAAS01114966};
CC -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000256|SAAS:SAAS01070220}.
CC -!- CAUTION: The sequence shown here is derived from an
CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC preliminary data. {ECO:0000313|EMBL:KRM88817.1}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC -----------------------------------------------------------------------
DR EMBL; AYYX01000020; KRM88817.1; -; Genomic_DNA.
DR RefSeq; WP_034995140.1; NZ_AYYX01000020.1.
DR STRING; 1133569.AHYZ01000194_gene2097; -.
DR EnsemblBacteria; KRM88817; KRM88817; FD21_GL000754.
DR PATRIC; fig|1133569.4.peg.815; -.
DR Proteomes; UP000051576; 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 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 {ECO:0000256|HAMAP-Rule:MF_00165,
KW ECO:0000256|SAAS:SAAS01070209};
KW Complete proteome {ECO:0000313|Proteomes:UP000051576};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:KRM88817.1};
KW Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165,
KW ECO:0000256|SAAS:SAAS01070211};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165,
KW ECO:0000256|SAAS:SAAS01070205};
KW Reference proteome {ECO:0000313|Proteomes:UP000051576};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW ECO:0000256|SAAS:SAAS01070204}.
FT DOMAIN 8 198 Thymidylate_kin. {ECO:0000259|Pfam:
FT PF02223}.
FT NP_BIND 10 17 ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ SEQUENCE 213 AA; 24031 MW; 50DFC5B18B9D68CB CRC64;
MEGKFVTLEG LDGSGKTTVL RKLIETLNEQ QRHRIVVTRE PGGNQIAEKI RQLLLDSNSL
KMDSRTEALL YAAARRQHLV ENVLPALAAG KIIFCDRYVD SSIAYQGAGR QLGETAIAEL
NQFATAGLQA DLTLYFDLPP QVGLQRINHF RQDQINRLDQ EKIDFYQRVR ASYLRLVAEE
PKRVIKINAA TALVNVVEQT RQILKEHLPE LLG
//
