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Database: UniProt
Entry: C5B1U6_METEA
LinkDB: C5B1U6_METEA
Original site: C5B1U6_METEA 
ID   C5B1U6_METEA            Unreviewed;       295 AA.
AC   C5B1U6;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   OrderedLocusNames=MexAM1_META1p1918 {ECO:0000313|EMBL:ACS39730.1};
OS   Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS   9133 / AM1) (Methylobacterium extorquens).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=272630 {ECO:0000313|EMBL:ACS39730.1, ECO:0000313|Proteomes:UP000009081};
RN   [1] {ECO:0000313|EMBL:ACS39730.1, ECO:0000313|Proteomes:UP000009081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
RC   {ECO:0000313|Proteomes:UP000009081};
RX   PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA   Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA   Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA   Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA   Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA   Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA   Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA   Lidstrom M.E.;
RT   "Methylobacterium genome sequences: a reference blueprint to investigate
RT   microbial metabolism of C1 compounds from natural and industrial sources.";
RL   PLoS ONE 4:E5584-E5584(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC         N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC         COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC         Evidence={ECO:0000256|ARBA:ARBA00001279};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594}.
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DR   EMBL; CP001510; ACS39730.1; -; Genomic_DNA.
DR   RefSeq; WP_012752700.1; NC_012808.1.
DR   AlphaFoldDB; C5B1U6; -.
DR   STRING; 272630.MexAM1_META1p1918; -.
DR   REBASE; 21143; M.MexAMORF1918P.
DR   KEGG; mea:Mex_1p1918; -.
DR   eggNOG; COG0338; Bacteria.
DR   HOGENOM; CLU_063430_1_1_5; -.
DR   OrthoDB; 9805629at2; -.
DR   Proteomes; UP000009081; Chromosome.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR   InterPro; IPR012263; M_m6A_EcoRV.
DR   InterPro; IPR012327; MeTrfase_D12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR30481:SF4; D12 CLASS N6 ADENINE-SPECIFIC DNA METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR   Pfam; PF02086; MethyltransfD12; 1.
DR   PIRSF; PIRSF000398; M_m6A_EcoRV; 1.
DR   PRINTS; PR00505; D12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:ACS39730.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009081};
KW   Transferase {ECO:0000313|EMBL:ACS39730.1}.
FT   BINDING         20
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         24
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         65
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         198
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
SQ   SEQUENCE   295 AA;  32888 MW;  FEF7C41699FC8C09 CRC64;
     MSAEVVALRP GAPRRPMVRW LGGKWTMGPW VISHMPPHEC YVEPFGGSAS VLMRKARAPV
     EVLGDLDDEL LTLYHVVRDP VLAGRLYLAV TYTPFSDAEY RLAMRRLPAD ADPVERARRL
     VARHAMQVSP DVRQSATAGS GFRRYSGSSR RIAAMDWARF PDALEAITAR LQGVVIERAP
     AVETIRRHDR PGALHYVDPP YVHSTRAEVR KGYAHEMTDA QHEELLDCLL GLQGMAVVSG
     YASPLYDEAL AGWRRVTRIV SDHARQRREE VLWISPNAVA ASDSSAKADR QASLF
//
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