ID   ADOM_BPT3               Reviewed;         152 AA.
AC   P07693; Q8W5V0;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=S-adenosyl-L-methionine hydrolase;
DE            Short=ADOMetase;
DE            Short=Adenosylmethionine hydrolase;
DE            Short=SAMase;
DE            EC=3.3.1.2;
OS   Enterobacteria phage T3 (Bacteriophage T3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Autographiviridae; Studiervirinae; Teetrevirus;
OC   Escherichia virus T3.
OX   NCBI_TaxID=10759;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3547328; DOI=10.1093/nar/15.2.717;
RA   Hughes J.A., Brown L.R., Ferro A.J.;
RT   "Nucleotide sequence and analysis of the coliphage T3 S-adenosylmethionine
RT   hydrolase gene and its surrounding ribonuclease III processing sites.";
RL   Nucleic Acids Res. 15:717-729(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Luria {ECO:0000312|EMBL:CAC86259.1};
RX   PubMed=12079351; DOI=10.1016/s0022-2836(02)00384-4;
RA   Pajunen M.I., Elizondo M.R., Skurnik M., Kieleczawa J., Molineux I.J.;
RT   "Complete nucleotide sequence and likely recombinatorial origin of
RT   bacteriophage T3.";
RL   J. Mol. Biol. 319:1115-1132(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Li S.;
RT   "Resequencing of Bacteriophage T3.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION.
RX   PubMed=781304; DOI=10.1128/jvi.19.1.136-145.1976;
RA   Studier F.W., Movva N.R.;
RT   "SAMase gene of bacteriophage T3 is responsible for overcoming host
RT   restriction.";
RL   J. Virol. 19:136-145(1976).
CC   -!- FUNCTION: Cleaves of S-adenosylmethionine and may therefore prevent
CC       both modification and degradation of viral DNA by the host restriction-
CC       modification complex. {ECO:0000269|PubMed:781304}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-adenosyl-L-methionine = H(+) + L-homoserine + S-
CC         methyl-5'-thioadenosine; Xref=Rhea:RHEA:14645, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:57476,
CC         ChEBI:CHEBI:59789; EC=3.3.1.2;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA28478.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X04791; CAA28477.1; -; Genomic_DNA.
DR   EMBL; X04791; CAA28478.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AJ318471; CAC86259.1; -; Genomic_DNA.
DR   EMBL; KC960671; AGM10703.1; -; Genomic_DNA.
DR   PIR; A26441; DABPT3.
DR   RefSeq; NP_523296.1; NC_003298.1.
DR   RefSeq; NP_523297.1; NC_003298.1.
DR   PDB; 7OCK; EM; 3.60 A; A/J/K/L=1-152.
DR   PDBsum; 7OCK; -.
DR   SMR; P07693; -.
DR   GeneID; 927434; -.
DR   GeneID; 927435; -.
DR   KEGG; vg:927434; -.
DR   KEGG; vg:927435; -.
DR   BRENDA; 4.4.1.B4; 731.
DR   Proteomes; UP000002092; Genome.
DR   Proteomes; UP000229888; Genome.
DR   GO; GO:0047626; F:adenosylmethionine hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0099018; P:evasion by virus of host restriction-modification system; IEA:UniProtKB-KW.
DR   InterPro; IPR016290; S-AdoMet_hydrolase.
DR   PIRSF; PIRSF001110; SAM_hydrolase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Host-virus interaction; Hydrolase; Reference proteome;
KW   Restriction-modification system evasion by virus; S-adenosyl-L-methionine.
FT   CHAIN           1..152
FT                   /note="S-adenosyl-L-methionine hydrolase"
FT                   /id="PRO_0000106548"
FT   CONFLICT        9
FT                   /note="H -> N (in Ref. 3; AGM10703 and 2; CAC86259)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   152 AA;  17035 MW;  0B28B872A91DD63C CRC64;
     MIFTKEPAHV FYVLVSAFRS NLCDEVNMSR HRHMVSTLRA APGLYGSVES TDLTGCYREA
     ISSAPTEEKT VRVRCKDKAQ ALNVARLACN EWEQDCVLVY KSQTHTAGLV YAKGIDGYKA
     ERLPGSFQEV PKGAPLQGCF TIDEFGRRWQ VQ