HMUDK_BPPM6
ID HMUDK_BPPM6 Reviewed; 187 AA.
AC P0DTK5;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 1.
DT 03-AUG-2022, entry version 1.
DE RecName: Full=5-hmdU DNA kinase {ECO:0000303|PubMed:34522950};
DE AltName: Full=5-hydroxymethyluracil DNA kinase {ECO:0000303|PubMed:34522950};
DE AltName: Full=P-loop kinase {ECO:0000303|PubMed:34522950};
DE AltName: Full=gp54 {ECO:0000303|PubMed:34522950};
OS Pseudomonas phage M6.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Yuavirus.
OX NCBI_TaxID=2911432;
OH NCBI_TaxID=287; Pseudomonas aeruginosa.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16428425; DOI=10.1128/jb.188.3.1184-1187.2006;
RA Kwan T., Liu J., Dubow M., Gros P., Pelletier J.;
RT "Comparative genomic analysis of 18 Pseudomonas aeruginosa
RT bacteriophages.";
RL J. Bacteriol. 188:1184-1187(2006).
RN [2]
RP FUNCTION.
RX PubMed=29555775; DOI=10.1073/pnas.1714812115;
RA Lee Y.J., Dai N., Walsh S.E., Mueller S., Fraser M.E., Kauffman K.M.,
RA Guan C., Correa I.R. Jr., Weigele P.R.;
RT "Identification and biosynthesis of thymidine hypermodifications in the
RT genomic DNA of widespread bacterial viruses.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E3116-E3125(2018).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=34522950; DOI=10.1093/nar/gkab781;
RA Lee Y.J., Dai N., Mueller S.I., Guan C., Parker M.J., Fraser M.E.,
RA Walsh S.E., Sridar J., Mulholland A., Nayak K., Sun Z., Lin Y.C.,
RA Comb D.G., Marks K., Gonzalez R., Dowling D.P., Bandarian V., Saleh L.,
RA Correa I.R., Weigele P.R.;
RT "Pathways of thymidine hypermodification.";
RL Nucleic Acids Res. 0:0-0(2021).
CC -!- FUNCTION: Phosphorylates 5-hydroxymethyluracil (5hmdU) into 5-
CC phosphomethyl-2'-deoxyuridine (5-PmdU) on DNA as a step in the pathway
CC leading to thymidine hypermodifications in the viral genome
CC (PubMed:34522950). The phosphate is added internally to the DNA polymer
CC (PubMed:34522950). Also transfers glutamate to 5-
CC pyrophosphoryloxymethyldeoxyuridine (5-PPmdU) to produce 5-Nalpha-
CC glyutamylthymidine (Nalpha-GluT). As a final result of the pathway of
CC hypermodification, 5-aminoethyl-2'-deoxyuridine (5-NedU) substitutes
CC for about 30% of thymidines in the viral DNA (PubMed:34522950,
CC PubMed:29555775). These modifications probably prevent degradation of
CC viral genome by the host restriction-modification antiviral defense
CC system (PubMed:34522950). {ECO:0000269|PubMed:29555775,
CC ECO:0000269|PubMed:34522950}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-hydroxymethyl-dUMP in DNA + ATP = 5-phosphomethyl-dUMP in
CC DNA + ADP + H(+); Xref=Rhea:RHEA:71543, Rhea:RHEA-COMP:18039,
CC Rhea:RHEA-COMP:18041, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:190917, ChEBI:CHEBI:190918, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:34522950};
CC -!- SIMILARITY: Belongs to the thymidylate kinase family. 5-hmdU DNA kinase
CC subfamily. {ECO:0000305}.
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DR EMBL; DQ163916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; YP_001294562.1; NC_007809.1.
PE 1: Evidence at protein level;
KW Host-virus interaction; Kinase;
KW Restriction-modification system evasion by virus; Transferase.
FT CHAIN 1..187
FT /note="5-hmdU DNA kinase"
FT /id="PRO_0000456265"
SQ SEQUENCE 187 AA; 20325 MW; 42917748EA5E8566 CRC64;
MKYINVRGCN GSGKTTLLRC LARDPLCRVI NVIVPDHKPI PVTYAPDGIA IIGDYTPAAA
GATTAGLDRI KTQAAAKAVA ELVGRDPDVK AVLFEGVVVS TIYGPWQEWS KANGGMIWAF
LDTPLEVCLK RIQERNGGKP IKEDQVADKH RTIARVRDKA LADGETVRDI HWETALKDIK
AVIENLG