DNMK_BPT4
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 03-AUG-2022, entry version 113.
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 Caudovirales; Myoviridae; 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}.
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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 EvolutionaryTrace; P04531; -.
DR Proteomes; UP000009087; Genome.
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; -; 1.
DR InterPro; IPR023191; DNMP_kinase_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 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
