ID   PLP_BPPM6               Reviewed;         278 AA.
AC   P0DTK8;
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=Glycyl-dTMP PLP-dependent decarboxylase {ECO:0000305};
DE   AltName: Full=gp52 {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: Converts 5-Calpha-glycinylthymidine (Calpha-GlyT) into 5-
CC       aminoethyl-2'-deoxyuridine (5-NedU) as a step in the pathway leading to
CC       thymidine hypermodifications in the viral genome (PubMed:34522950). As
CC       a final result of the pathway of hypermodification, 5-aminoethyl-2'-
CC       deoxyuridine (5-NedU) substitutes for about 30% of thymidines in the
CC       viral DNA (PubMed:34522950, PubMed:29555775). These modifications
CC       probably prevent degradation of viral genome by the host restriction-
CC       modification antiviral defense system (PubMed:34522950).
CC       {ECO:0000269|PubMed:29555775, ECO:0000269|PubMed:34522950}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-C(alpha)-glycyl-dTMP in DNA + H(+) = 5-aminoethyl-dUMP in
CC         DNA + CO2; Xref=Rhea:RHEA:71555, Rhea:RHEA-COMP:18042, Rhea:RHEA-
CC         COMP:18043, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:190924,
CC         ChEBI:CHEBI:190925; Evidence={ECO:0000269|PubMed:34522950};
CC   -!- SIMILARITY: Belongs to the pyridoxal-phosphate-dependent
CC       aminodecarboxylase family. {ECO:0000305}.
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DR   EMBL; DQ163916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; YP_001294560.1; NC_007809.1.
PE   1: Evidence at protein level;
KW   Decarboxylase; Host-virus interaction; Lyase;
KW   Restriction-modification system evasion by virus.
FT   CHAIN           1..278
FT                   /note="Glycyl-dTMP PLP-dependent decarboxylase"
FT                   /id="PRO_0000456277"
SQ   SEQUENCE   278 AA;  30650 MW;  A13DAE6D2150288E CRC64;
     MIVNNTPVET YELNGVPILV KREDLCAPLP GPSFSKIRGV VAHIKNRPET TIGCLDTYHS
     KAGWAVAYVC QQLGKQAVDY WPRFKRDGAA DAPRVQQQHA RQLGADLVDI PAGRSAILYH
     TAKKHLRENY HDSYLMPNAL KLPESITENA AEAVRTAPHL PDSGTLVISI SSGTVAAGVL
     KGFEEAGLLR NYNVILHMGY SRSQDATREY IEKAAGLTLG DRIKFIDEGY GYADAARDAS
     APFPCNPFYD LKAWKWLSNP TNLETILDGP IVFWNIGE