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Database: UniProt/TrEMBL
Entry: A4WRX3_RHOS5
LinkDB: A4WRX3_RHOS5
Original site: A4WRX3_RHOS5 
ID   A4WRX3_RHOS5            Unreviewed;       217 AA.
AC   A4WRX3;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   29-OCT-2014, entry version 48.
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=Rsph17025_1236 {ECO:0000313|EMBL:ABP70137.1};
OS   Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=349102 {ECO:0000313|EMBL:ABP70137.1, ECO:0000313|Proteomes:UP000000234};
RN   [1] {ECO:0000313|EMBL:ABP70137.1, ECO:0000313|Proteomes:UP000000234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17025 / ATH 2.4.3 {ECO:0000313|Proteomes:UP000000234};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.,
RA   Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC
RT   17025.";
RL   Submitted (APR-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:0000256|HAMAP-
CC       Rule:MF_00165}.
CC   -!- CATALYTIC ACTIVITY: ATP + dTMP = ADP + dTDP. {ECO:0000256|HAMAP-
CC       Rule:MF_00165, ECO:0000256|SAAS:SAAS00031904}.
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00165}.
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DR   EMBL; CP000661; ABP70137.1; -; Genomic_DNA.
DR   RefSeq; YP_001167442.1; NC_009428.1.
DR   STRING; 349102.Rsph17025_1236; -.
DR   EnsemblBacteria; ABP70137; ABP70137; Rsph17025_1236.
DR   GeneID; 5084409; -.
DR   KEGG; rsq:Rsph17025_1236; -.
DR   PATRIC; 23160673; VBIRhoSph94549_1269.
DR   eggNOG; COG0125; -.
DR   HOGENOM; HOG000229078; -.
DR   KO; K00943; -.
DR   OMA; EPGGCPI; -.
DR   OrthoDB; EOG64JFSH; -.
DR   BioCyc; RSPH349102:GHE1-2564-MONOMER; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00165; Thymidylate_kinase; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR018095; Thymidylate_kin_CS.
DR   InterPro; IPR018094; Thymidylate_kinase.
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:SAAS00031914};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000234};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS00031912};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS00031908};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS00031897};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS00031919}.
FT   NP_BIND      13     20       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   217 AA;  23026 MW;  CC388D8F45DA116B CRC64;
     MRAQGGLFLA VEGIDGSGKS GIVQHLAARL RAHGREVVVT REPGGTPEGE AIRGLVLAGA
     DEAWDPMAEL LLMTAARVQH VRRVIAPALE AGSVVLSDRY AGSTLAYQGT GRGLSESFIR
     ALHAEATGDL WPDLTLILDL DAATGLARSR RRLTGSAIDE GRFESLDLAF HERIRQSFRA
     QAARDPARHA VIDASGTPEQ VQARALAALE PVLAAAR
//
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