ID   FADL_BPPAM              Reviewed;         286 AA.
AC   A0A0S0N8M3;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   17-FEB-2016, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Flavin-dependent lyase {ECO:0000303|PubMed:34522950};
DE   AltName: Full=gp47 {ECO:0000303|PubMed:34522950};
GN   ORFNames=PaMx11_47 {ECO:0000312|EMBL:ALH23721.1};
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: Catalyzes the cleavage of the N-Calpha bond of glycine in
CC       Nalpha-GlyT to produce 5-aminomethyl-2'-deoxyuridine (5-NmdU) on DNA as
CC       a step in the pathway leading to thymidine hypermodifications in the
CC       viral genome (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-N(alpha)-glycyl-dTMP in DNA + A + H2O = 5-aminomethyl-dUMP
CC         in DNA + AH2 + glyoxylate; Xref=Rhea:RHEA:71559, Rhea:RHEA-
CC         COMP:18040, Rhea:RHEA-COMP:18044, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:190919, ChEBI:CHEBI:190926;
CC         Evidence={ECO:0000269|PubMed:34522950};
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DR   EMBL; JQ067087; ALH23721.1; -; Genomic_DNA.
DR   RefSeq; YP_009196300.1; NC_028770.1.
DR   GeneID; 26623525; -.
DR   KEGG; vg:26623525; -.
DR   Proteomes; UP000204009; Genome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Host-virus interaction; Lyase;
KW   Restriction-modification system evasion by virus.
FT   CHAIN           1..286
FT                   /note="Flavin-dependent lyase"
FT                   /id="PRO_0000456279"
SQ   SEQUENCE   286 AA;  30710 MW;  98F06403650F21E4 CRC64;
     MKTDVIVVGA GLFGSIAAKA LAQAGLAVVG VDDSRPGAGS LPAACLMKPS WFSSMGKDKF
     EPSLELLDRI YGVKDISFKV GLLRATVHWC DPAQILGDEE VPVYREKVTA LTRTSSGWAV
     SLEGREAALE ARSVVVAAGV WTSELVRSQA LGGLVGRAGV AFRWQDMQLE EQFISPWAPY
     RQTVGFNISP TEVWVGDGSA IKPENWNQDR QNVSYSRCAQ AIDRAGFGDQ EAGRVKALYG
     IRPYIAGVKP CLLEEVEPGL WALTGGAKNG TISAGWAASE LVRRIK