ID   AT_BPPAM                Reviewed;         140 AA.
AC   A0A0S0MX59;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   17-FEB-2016, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=5-NmdU N-acetyltransferase {ECO:0000303|PubMed:34522950};
GN   Name=gp48 {ECO:0000303|PubMed:34522950};
GN   and
GN   ORFNames=PaMx11_48 {ECO:0000312|EMBL:ALH23722.1};
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: Acetylates 5-aminomethyl-2'-deoxyuridine (5-NmdU) to produce
CC       5-acetylaminomethyl-2'-deoxyuridine (5-AcNmdU) on DNA 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-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-aminomethyl-dUMP in DNA + acetyl-CoA = 5-acetylaminomethyl-
CC         dUMP in DNA + CoA + H(+); Xref=Rhea:RHEA:71563, Rhea:RHEA-COMP:18044,
CC         Rhea:RHEA-COMP:18048, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:190926, ChEBI:CHEBI:190928;
CC         Evidence={ECO:0000269|PubMed:34522950};
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR   EMBL; JQ067087; ALH23722.1; -; Genomic_DNA.
DR   RefSeq; YP_009196301.1; NC_028770.1.
DR   GeneID; 26623526; -.
DR   KEGG; vg:26623526; -.
DR   Proteomes; UP000204009; Genome.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Host-virus interaction;
KW   Restriction-modification system evasion by virus; Transferase.
FT   CHAIN           1..140
FT                   /note="5-NmdU N-acetyltransferase"
FT                   /id="PRO_0000456280"
FT   DOMAIN          2..140
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   140 AA;  15969 MW;  38AB5248ABE2B000 CRC64;
     MIVVRKALPE EHKEILQVAK QSKYTKDFSN QVMFSSEAAY NKGWIHVAEH EGEIRGFYCI
     REKVRAPETV LYFIGVAQEA KGLGLGKKLI EHIMATTRHR RLTLNVNKQN EEARAFYDRL
     GFTVAGESLG GEGLALFKEW