ID   GLYDT_BPPM6             Reviewed;         291 AA.
AC   P0DTK6;
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=Glycinyltransferase {ECO:0000305};
DE   AltName: Full=Amino acid:DNA transferase {ECO:0000303|PubMed:34522950};
DE            Short=AADT {ECO:0000303|PubMed:34522950};
DE   AltName: Full=gp51 {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, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-243 AND CYS-247.
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: Transfers glycine to 5-phosphomethyl-2'-deoxyuridine (5-PmdU)
CC       to produce 5-Nalpha-glycinylthymidine (Nalpha-GlyT) as a step in the
CC       pathway leading to thymidine hypermodifications in the viral genome
CC       (PubMed:34522950). 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-phosphomethyl-dUMP in DNA + glycine = 5-N(alpha)-glycyl-dTMP
CC         in DNA + phosphate; Xref=Rhea:RHEA:71547, Rhea:RHEA-COMP:18039,
CC         Rhea:RHEA-COMP:18040, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:190918, ChEBI:CHEBI:190919;
CC         Evidence={ECO:0000269|PubMed:34522950};
CC   -!- SIMILARITY: Belongs to the thymidine aminotransferase family.
CC       {ECO:0000305}.
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DR   EMBL; DQ163916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; YP_001294559.1; NC_007809.1.
PE   1: Evidence at protein level;
KW   Host-virus interaction; Restriction-modification system evasion by virus;
KW   Transferase.
FT   CHAIN           1..291
FT                   /note="Glycinyltransferase"
FT                   /id="PRO_0000456272"
FT   ACT_SITE        243
FT                   /evidence="ECO:0000305|PubMed:34522950"
FT   MUTAGEN         243
FT                   /note="E->A: Complete loss of enzymatic activity."
FT                   /evidence="ECO:0000269|PubMed:34522950"
FT   MUTAGEN         247
FT                   /note="C->A: Complete loss of enzymatic activity."
FT                   /evidence="ECO:0000269|PubMed:34522950"
SQ   SEQUENCE   291 AA;  33462 MW;  5E6FA65ADF204146 CRC64;
     MSRNYPRLDI ETFGRHLITT GDLDPIYTAL VRAEEAGDFS VPQLCRWLLG YWCYYHAGVA
     SFLSEKEGEE FWHWMMVAAR NEEETPAGGR WPRGHERRHY RAKIAVDSVT SLQARYGDRP
     ENMALYVGAR ATEDERLPFR TVSARAQEHN GFGPWIGFKI ADMMDRVMEV PVDFDNAAVF
     MFKDPEKAAM MLWEQREAHK YPENAKPKRE AILSGVADYL IGRFADLAAP PLSDRPVNIQ
     EVETVLCKWK SHMNGHYPLW NDIREINGGL EPWAGRCSAA RAFLNHMPKE Q