ID DNMK_BPT4 Reviewed; 241 AA. AC P04531; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 24-JAN-2024, entry version 117. DE RecName: Full=Deoxynucleotide monophosphate kinase; DE Short=DNK; DE Short=dNMP kinase; DE EC=2.7.4.13; DE AltName: Full=Gp1; GN Name=1; OS Enterobacteria phage T4 (Bacteriophage T4). OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Straboviridae; Tevenvirinae; Tequatrovirus. OX NCBI_TaxID=10665; OH NCBI_TaxID=562; Escherichia coli. RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=4057254; DOI=10.1016/0022-2836(85)90071-3; RA Broida J., Abelson J.; RT "Sequence organization and control of transcription in the bacteriophage T4 RT tRNA region."; RL J. Mol. Biol. 185:545-563(1985). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003; RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.; RT "Bacteriophage T4 genome."; RL Microbiol. Mol. Biol. Rev. 67:86-156(2003). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 148-241. RX PubMed=7063418; DOI=10.1093/nar/10.3.1105; RA Herrmann R.; RT "Nucleotide sequence of the bacteriophage T4 gene 57 and a deduced amino RT acid sequence."; RL Nucleic Acids Res. 10:1105-1112(1982). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27. RX PubMed=2740234; DOI=10.1093/nar/17.11.4392; RA Koch T., Lamm N., Rueger W.; RT "Sequencing, cloning and overexpression of genes of bacteriophage T4 RT between map positions 74.325 and 77.184."; RL Nucleic Acids Res. 17:4392-4392(1989). RN [5] RP FUNCTION. RX PubMed=5338507; DOI=10.1016/s0021-9258(18)99587-6; RA Duckworth D.H., Bessman M.J.; RT "The enzymology of virus-infected bacteria. X. A biochemical-genetic study RT of the deoxynucleotide kinase induced by wild type and amber mutants of RT phage T4."; RL J. Biol. Chem. 242:2877-2885(1967). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=8670851; DOI=10.1002/j.1460-2075.1996.tb00717.x; RA Teplyakov A., Sebastiao P., Obmolova G., Perrakis A., Brush G.S., RA Bessman M.J., Wilson K.S.; RT "Crystal structure of bacteriophage T4 deoxynucleotide kinase with its RT substrates dGMP and ATP."; RL EMBO J. 15:3487-3497(1996). CC -!- FUNCTION: Phosphorylates dGMP, dTMP and 5-hydroxymethyl-dCMP while CC excluding dCMP and dAMP. The phosphorylation of 5-hydroxymethyl-dCMP CC represents the first step in the replacement of cytosine by CC hydroxymethylcytosine in new viral DNA genomes. CC {ECO:0000269|PubMed:5338507}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-phosphate + ATP = a 2'- CC deoxyribonucleoside 5'-diphosphate + ADP; Xref=Rhea:RHEA:11216, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:65317, ChEBI:CHEBI:73316, CC ChEBI:CHEBI:456216; EC=2.7.4.13; CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the dNMP kinase family. {ECO:0000305}. 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; X03016; CAA26800.1; -; Genomic_DNA. DR EMBL; AF158101; AAD42414.1; -; Genomic_DNA. DR EMBL; X14845; CAA32953.1; -; Genomic_DNA. DR PIR; C92919; KIBPD4. DR RefSeq; NP_049752.1; NC_000866.4. DR PDB; 1DEK; X-ray; 2.00 A; A/B=1-241. DR PDB; 1DEL; X-ray; 2.20 A; A/B=1-241. DR PDBsum; 1DEK; -. DR PDBsum; 1DEL; -. DR SMR; P04531; -. DR DrugBank; DB04457; 2'-Deoxyguanosine-5'-Monophosphate. DR DrugBank; DB03661; L-cysteic acid. DR GeneID; 1258557; -. DR KEGG; vg:1258557; -. DR OrthoDB; 14006at10239; -. DR EvolutionaryTrace; P04531; -. DR Proteomes; UP000009087; Segment. DR GO; GO:0047507; F:(deoxy)nucleoside-phosphate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR Gene3D; 1.10.238.70; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR048444; DNMK. DR InterPro; IPR023191; DNMP_kinase_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF21448; DNMK; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1..241 FT /note="Deoxynucleotide monophosphate kinase" FT /id="PRO_0000164948" FT STRAND 2..7 FT /evidence="ECO:0007829|PDB:1DEK" FT HELIX 14..24 FT /evidence="ECO:0007829|PDB:1DEK" FT STRAND 27..29 FT /evidence="ECO:0007829|PDB:1DEK" FT HELIX 34..47 FT /evidence="ECO:0007829|PDB:1DEK" FT TURN 48..50 FT /evidence="ECO:0007829|PDB:1DEL" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:1DEK" FT HELIX 58..61 FT /evidence="ECO:0007829|PDB:1DEK" FT TURN 62..65 FT /evidence="ECO:0007829|PDB:1DEK" FT HELIX 76..91 FT /evidence="ECO:0007829|PDB:1DEK" FT STRAND 101..106 FT /evidence="ECO:0007829|PDB:1DEK" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:1DEK" FT HELIX 112..123 FT /evidence="ECO:0007829|PDB:1DEK" FT HELIX 131..139 FT /evidence="ECO:0007829|PDB:1DEK" FT TURN 140..142 FT /evidence="ECO:0007829|PDB:1DEK" FT HELIX 143..146 FT /evidence="ECO:0007829|PDB:1DEK" FT HELIX 151..163 FT /evidence="ECO:0007829|PDB:1DEK" FT STRAND 169..173 FT /evidence="ECO:0007829|PDB:1DEK" FT HELIX 179..187 FT /evidence="ECO:0007829|PDB:1DEK" FT STRAND 191..196 FT /evidence="ECO:0007829|PDB:1DEK" FT HELIX 207..209 FT /evidence="ECO:0007829|PDB:1DEK" FT STRAND 219..222 FT /evidence="ECO:0007829|PDB:1DEK" FT HELIX 227..239 FT /evidence="ECO:0007829|PDB:1DEK" SQ SEQUENCE 241 AA; 27329 MW; 61AD2375CC94BDE8 CRC64; MKLIFLSGVK RSGKDTTADF IMSNYSAVKY QLAGPIKDAL AYAWGVFAAN TDYPCLTRKE FEGIDYDRET NLNLTKLEVI TIMEQAFCYL NGKSPIKGVF VFDDEGKESV NFVAFNKITD VINNIEDQWS VRRLMQALGT DLIVNNFDRM YWVKLFALDY LDKFNSGYDY YIVPDTRQDH EMDAARAMGA TVIHVVRPGQ KSNDTHITEA GLPIRDGDLV ITNDGSLEEL FSKIKNTLKV L //