ID   RSAMI_BPPM6             Reviewed;         480 AA.
AC   P0DTK7;
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=Radical SAM Nalpha-GlyT isomerase {ECO:0000303|PubMed:34522950};
DE   AltName: Full=gp53 {ECO:0000303|PubMed:34522950};
DE   AltName: Full=rSAM glycinyl-thymine isomerase {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: Isomerizes 5-N-alpha-glycinylthymidine (Nalpha-GlyT) into 5-
CC       Calpha-glycinylthymidine (Calpha-GlyT) as a step in the pathway leading
CC       to thymidine hypermodifications in the viral genome (PubMed:34522950).
CC       As 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-N(alpha)-glycyl-dTMP in DNA + AH2 + S-adenosyl-L-methionine
CC         = 5'-deoxyadenosine + 5-C(alpha)-glycyl-dTMP in DNA + A + H(+) + L-
CC         methionine; Xref=Rhea:RHEA:71551, Rhea:RHEA-COMP:18040, Rhea:RHEA-
CC         COMP:18042, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:190919, ChEBI:CHEBI:190924;
CC         Evidence={ECO:0000269|PubMed:34522950};
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DR   EMBL; DQ163916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; YP_001294561.1; NC_007809.1.
PE   1: Evidence at protein level;
KW   Host-virus interaction; Iron; Iron-sulfur; Isomerase; Metal-binding;
KW   Restriction-modification system evasion by virus.
FT   CHAIN           1..480
FT                   /note="Radical SAM Nalpha-GlyT isomerase"
FT                   /id="PRO_0000456276"
FT   BINDING         125
FT                   /ligand="iron-sulfur cluster"
FT                   /ligand_id="ChEBI:CHEBI:30408"
FT                   /evidence="ECO:0000305|PubMed:34522950"
FT   BINDING         129
FT                   /ligand="iron-sulfur cluster"
FT                   /ligand_id="ChEBI:CHEBI:30408"
FT                   /evidence="ECO:0000305|PubMed:34522950"
FT   BINDING         132
FT                   /ligand="iron-sulfur cluster"
FT                   /ligand_id="ChEBI:CHEBI:30408"
FT                   /evidence="ECO:0000305|PubMed:34522950"
SQ   SEQUENCE   480 AA;  54374 MW;  FDFE73DE12778F26 CRC64;
     MDHAAWLNEE TGEAAQEAYK YFMRPDPNQR EFLGPIEEED DPLTGMRAKF RMAKVGMVRN
     AKDEDKKEVK VYLGFNDVTY LPHIRIPNAK PLQGWYQDKH NDKRGSRARP CFSEAILTEP
     YGGYCTVGCA FCYVNSGFRG YRGTGLISVP VNYGEQVRNM LSKSRTSAAG YFSSFTDPFL
     PIEDVYHNTQ QGAEAFVELG LPIFFLSRLS YPSWAIDLLK RNPYSYAQKS LNTGNDRDWH
     KLSPGAISLQ DHIDEIAELR RQGIYTSIQV NPVVPGIVTH DDIRHLFERL AAVGNNHVIV
     KFVEAGYSWA PAMIERLHKR FGPERTKAFT DLFTENQAGA QKTIAEPYRV EAHQLYRKWA
     TELGMTYATC YEYRRGKPGT GEPAWLSMGR EMITADQCHG QRVPMFTRTD LDQPFQEVKE
     CAPTGCLHCA DDNEGKPRCG SELFGAAKAL RSPDFKKIVE PTPPEEDGGE RKIIPITQID