ID   PLP_BPSAV               Reviewed;         424 AA.
AC   E1XTJ1;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=O-seryl-dTMP PLP-dependent decarboxylase {ECO:0000305};
GN   Name=gp226 {ECO:0000303|PubMed:34522950};
GN   and
GN   ORFNames=Vi01_182 {ECO:0000312|EMBL:CBW38050.1};
OS   Salmonella phage ViI.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Ackermannviridae; Cvivirinae; Kuttervirus.
OX   NCBI_TaxID=1987993;
OH   NCBI_TaxID=90370; Salmonella typhi.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20817773; DOI=10.1128/jb.00659-10;
RA   Pickard D., Toribio A.L., Petty N.K., van Tonder A., Yu L., Goulding D.,
RA   Barrell B., Rance R., Harris D., Wetter M., Wain J., Choudhary J.,
RA   Thomson N., Dougan G.;
RT   "A conserved acetyl esterase domain targets diverse bacteriophages to the
RT   Vi capsular receptor of Salmonella enterica serovar Typhi.";
RL   J. Bacteriol. 192:5746-5754(2010).
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-O-serinylthymidine (O-SerT) into 5-aminoethoxy-2'-
CC       deoxymethyluridine (5-NeOmdU) 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-NeOmdU
CC       substitutes for about 40% of the thymidines in the viral DNA
CC       (PubMed:34522950, PubMed:29555775). These modifications probably
CC       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-O-(L-seryl)-dTMP in DNA + H(+) = 5-aminoethoxy-methyl-dUMP
CC         in DNA + CO2; Xref=Rhea:RHEA:71571, Rhea:RHEA-COMP:18046, Rhea:RHEA-
CC         COMP:18047, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:190922,
CC         ChEBI:CHEBI:190923; Evidence={ECO:0000269|PubMed:34522950};
CC   -!- SIMILARITY: Belongs to the pyridoxal-phosphate-dependent
CC       aminodecarboxylase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FQ312032; CBW38050.1; -; Genomic_DNA.
DR   Proteomes; UP000000339; Genome.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   SUPFAM; SSF53686; SSF53686; 1.
PE   1: Evidence at protein level;
KW   Decarboxylase; Host-virus interaction; Lyase; Reference proteome;
KW   Restriction-modification system evasion by virus.
FT   CHAIN           1..424
FT                   /note="O-seryl-dTMP PLP-dependent decarboxylase"
FT                   /id="PRO_0000456278"
SQ   SEQUENCE   424 AA;  48090 MW;  A02C9B38AA87769F CRC64;
     MNEPIDPKSF PSQPLSPYIP MHHIGKGPYK TIFNVLSLNR DHIHWEDYLY KHTPCELVAN
     PETNQQVWFK REDYFAPLSC YMNGKQGING SKLRQAIWLM VEHLKAGGSP DLIHGTVVGS
     PQSPMATAVS RHFGGKTTTV LGATKPTTCM NHDMVKMSAW FGSEFNFVGS GYNSTIQPRC
     KKLIEQQNPK AYYLEYGITL DHTLHSPERI AGFHMLGGEQ VANIPDHITD LIIPAGSCNS
     CTSILTGLAM HPKPNLKNVY LIGIGPNRLD FIESRLRIIG KQANLPHITD FTRCYHDNPD
     YVYGKKDLQH ASKSVSLAGL LMGIREKGES EITLPRFAVH HWDLHTTNWV RYNDLMDYQW
     GDIELHPRYE GKVMTWIQQH KPELLNENTL FWIVGSKPYI EPMKAACPEL SMPEQVPVNE
     FTPD