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Database: UniProt
Entry: A0A059FVQ4_9RHOB
LinkDB: A0A059FVQ4_9RHOB
Original site: A0A059FVQ4_9RHOB 
ID   A0A059FVQ4_9RHOB        Unreviewed;       219 AA.
AC   A0A059FVQ4;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   11-DEC-2019, entry version 25.
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=HJO_04905 {ECO:0000313|EMBL:KCZ94687.1};
OS   Hyphomonas johnsonii MHS-2.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Hyphomonadaceae; Hyphomonas.
OX   NCBI_TaxID=1280950 {ECO:0000313|EMBL:KCZ94687.1, ECO:0000313|Proteomes:UP000025171};
RN   [1] {ECO:0000313|EMBL:KCZ94687.1, ECO:0000313|Proteomes:UP000025171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHS-2 {ECO:0000313|EMBL:KCZ94687.1,
RC   ECO:0000313|Proteomes:UP000025171};
RX   PubMed=25070064; DOI=10.1007/s10482-014-0236-y;
RA   Li C., Lai Q., Li G., Dong C., Wang J., Liao Y., Shao Z.;
RT   "Hyphomonas beringensis sp. nov. and Hyphomonas chukchiensis sp. nov.,
RT   isolated from surface seawater of the Bering Sea and Chukchi Sea.";
RL   Antonie Van Leeuwenhoek 106:657-665(2014).
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; 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 EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KCZ94687.1}.
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DR   EMBL; ARYK01000001; KCZ94687.1; -; Genomic_DNA.
DR   STRING; 1280950.HJO_04905; -.
DR   EnsemblBacteria; KCZ94687; KCZ94687; HJO_04905.
DR   PATRIC; fig|1280950.3.peg.997; -.
DR   Proteomes; UP000025171; 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; IPR018095; Thymidylate_kin_CS.
DR   InterPro; IPR018094; Thymidylate_kinase.
DR   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR   PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070209};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000256|SAAS:SAAS01070206,
KW   ECO:0000313|EMBL:KCZ94687.1};
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:UP000025171};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204}.
FT   DOMAIN          13..202
FT                   /note="Thymidylate_kin"
FT                   /evidence="ECO:0000259|Pfam:PF02223"
FT   NP_BIND         15..22
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ   SEQUENCE   219 AA;  23665 MW;  ED30B345A3DEAF46 CRC64;
     MMADISRGRF ITLEGGEGTG KSTLQHALAE RLAANGIEVV ETREPGGTPL AESVRELALH
     PPRSEAWSPM AEALLMNAAR SDHLDKLIRP ALAAGKWVIC DRFADSTRVY QSVGAGVPMD
     FLKAMERSVL AQDVPDLTLV LDAPLDATAG RRKSRPGASD AFEVRPDDFH QAVRTGFIEL
     VRTEPARCRL LDASRPADEV ADAAWTELDR LLAARGQGA
//
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