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Database: UniProt
Entry: I1XKA7_METNJ
LinkDB: I1XKA7_METNJ
Original site: I1XKA7_METNJ 
ID   I1XKA7_METNJ            Unreviewed;       210 AA.
AC   I1XKA7;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   31-JUL-2019, 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   OrderedLocusNames=Q7A_2009 {ECO:0000313|EMBL:AFI84826.1};
GN   ORFNames=CDW43_09780 {ECO:0000313|EMBL:AUZ84846.1};
OS   Methylophaga nitratireducenticrescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Methylophaga.
OX   NCBI_TaxID=754476 {ECO:0000313|EMBL:AFI84826.1, ECO:0000313|Proteomes:UP000009144};
RN   [1] {ECO:0000313|EMBL:AFI84826.1, ECO:0000313|Proteomes:UP000009144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM1 {ECO:0000313|EMBL:AFI84826.1,
RC   ECO:0000313|Proteomes:UP000009144};
RX   PubMed=22815445; DOI=10.1128/JB.00726-12;
RA   Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT   "Complete genome sequences of Methylophaga sp. strain JAM1 and
RT   Methylophaga sp. strain JAM7.";
RL   J. Bacteriol. 194:4126-4127(2012).
RN   [2] {ECO:0000313|EMBL:AFI84826.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JAM1 {ECO:0000313|EMBL:AFI84826.1};
RX   PubMed=23148104; DOI=10.1099/ijs.0.044545-0;
RA   Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT   "Methylophaga nitratireducenticrescens sp. nov. and Methylophaga
RT   frappieri sp. nov., isolated from the biofilm of the methanol-fed
RT   denitrification system treating the seawater at the Montreal
RT   Biodome.";
RL   Int. J. Syst. Evol. Microbiol. 63:2216-2222(2013).
RN   [3] {ECO:0000313|EMBL:AFI84826.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JAM1 {ECO:0000313|EMBL:AFI84826.1};
RA   Villeneuve C., Villemur R.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AUZ84846.1, ECO:0000313|Proteomes:UP000238402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GP59 {ECO:0000313|EMBL:AUZ84846.1,
RC   ECO:0000313|Proteomes:UP000238402};
RA   Villemur R.;
RT   "The sequence of the genome of Methylophaga nitratireducenticrescens
RT   GP59 and its two plasmids.";
RL   Submitted (JUN-2017) 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-
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}.
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DR   EMBL; CP003390; AFI84826.1; -; Genomic_DNA.
DR   EMBL; CP021973; AUZ84846.1; -; Genomic_DNA.
DR   RefSeq; WP_014707194.1; NC_017857.3.
DR   STRING; 754476.Q7A_2009; -.
DR   EnsemblBacteria; AFI84826; AFI84826; Q7A_2009.
DR   KEGG; mej:Q7A_2009; -.
DR   PATRIC; fig|754476.3.peg.1987; -.
DR   KO; K00943; -.
DR   OMA; FLYTADH; -.
DR   OrthoDB; 1585072at2; -.
DR   BioCyc; MNIT754476:G1H54-1999-MONOMER; -.
DR   Proteomes; UP000009144; Chromosome.
DR   Proteomes; UP000238402; 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 {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070209};
KW   Complete proteome {ECO:0000313|Proteomes:UP000009144,
KW   ECO:0000313|Proteomes:UP000238402};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:AFI84826.1};
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   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204, ECO:0000313|EMBL:AFI84826.1}.
FT   DOMAIN        8    197       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND      10     17       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   210 AA;  23843 MW;  28AA9BCDB4BEAB10 CRC64;
     MNGKFISIEG IEGAGKSTQL QFIADYIRSH GKQVVVTREP GGTSLGEEIR EVLLKSTEQA
     MAEDTELLLM FAARAEHLQQ VILPALKRGD WVVSDRFVDA TFAYQGGGRG INEQRIKQLA
     DWTLQGCNTD VTFLFDLPVA LGQTRVEQRQ QQKDRFEQEK QVFFERVRNC YLARAEVEPK
     RIKRIDASQN IEAIQQQLKH QLAPLLEATL
//
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