ID   GLYDT_BPPAM             Reviewed;         292 AA.
AC   A0A0S0MVI5;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   17-FEB-2016, sequence version 1.
DT   03-AUG-2022, entry version 22.
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=gp46 {ECO:0000303|PubMed:34522950};
GN   ORFNames=PaMx11_46 {ECO:0000312|EMBL:ALH23720.1};
OS   Pseudomonas phage PaMx11.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Abidjanvirus.
OX   NCBI_TaxID=1175657;
OH   NCBI_TaxID=287; Pseudomonas aeruginosa.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22504803; DOI=10.1128/aem.00065-12;
RA   Sepulveda-Robles O., Kameyama L., Guarneros G.;
RT   "High Diversity and Novel Species of Pseudomonas aeruginosa
RT   Bacteriophages.";
RL   Appl. Environ. Microbiol. 78:4510-4515(2012).
RN   [2]
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: Transfers glycine to 5-phosphomethyl-2'-deoxyuridine (5-PmdU)
CC       to produce 5-Nalpha-glycinylthymidine (Nalpha-GlyT) on DNA as a step in
CC       the pathway leading to thymidine hypermodifications in the viral genome
CC       (PubMed:34522950). As a final result of the pathway of
CC       hypermodification, 5-acetylaminomethyl-2'-deoxyuridine (5-AcNmdU)
CC       substitutes for a subset of thymidines in the viral DNA
CC       (PubMed:34522950). These modifications probably prevent degradation of
CC       viral genome by the host restriction-modification antiviral defense
CC       system (PubMed:34522950). {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; JQ067087; ALH23720.1; -; Genomic_DNA.
DR   RefSeq; YP_009196299.1; NC_028770.1.
DR   GeneID; 26623524; -.
DR   KEGG; vg:26623524; -.
DR   Proteomes; UP000204009; Genome.
DR   InterPro; IPR040741; Alpha_GPT-Pplase2.
DR   Pfam; PF18724; aGPT-Pplase2; 1.
PE   1: Evidence at protein level;
KW   Host-virus interaction; Restriction-modification system evasion by virus;
KW   Transferase.
FT   CHAIN           1..292
FT                   /note="Glycinyltransferase"
FT                   /id="PRO_0000456273"
SQ   SEQUENCE   292 AA;  33417 MW;  0E530621B5CCDCEC CRC64;
     MSRNYEKLSI EEFGAHLLGT VDLDPIYLAL RRMELPEAQL NRWLLAYWCL YNGGEASYLS
     EFEGREFFEM LNHAAENVRE APIGGRWPRG AERRHWRGAQ ATSSVEYLID RYDDRPEDMA
     AYCAGQGGTF LEVTKRVQEH RLFGPWIGFK VADMVDRVLG KPVSFDNAAV FMFKDPYKAA
     CIQYEVNPNI PDHVLADGSV APRNRELVTP ETVHHVAQHL IEHFKGFQAP PLGDRPVNIQ
     EVETILCKWK SHQNGHYPLF KDIVEIREAA LPWAKVSKTA QAFFEAMPEV TQ