ID A7KGG3_KLEPN Unreviewed; 257 AA.
AC A7KGG3;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900, ECO:0000256|RuleBase:RU361257};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900, ECO:0000256|RuleBase:RU361257};
OS Klebsiella pneumoniae.
OG Plasmid pK29 {ECO:0000313|EMBL:ABQ03030.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573 {ECO:0000313|EMBL:ABQ03030.1};
RN [1] {ECO:0000313|EMBL:ABQ03030.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NK29 {ECO:0000313|EMBL:ABQ03030.1};
RC PLASMID=pK29 {ECO:0000313|EMBL:ABQ03030.1};
RX PubMed=17526756; DOI=10.1128/AAC.00167-07;
RA Chen Y.T., Lauderdale T.L., Liao T.L., Shiau Y.R., Shu H.Y., Wu K.M.,
RA Yan J.J., Su I.J., Tsai S.F.;
RT "Sequencing and comparative genomic analysis of pK29, a 269-kilobase
RT conjugative plasmid encoding CMY-8 and CTX-M-3 beta-lactamases in
RT Klebsiella pneumoniae.";
RL Antimicrob. Agents Chemother. 51:3004-3007(2007).
RN [2] {ECO:0000313|EMBL:ABQ03030.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NK29 {ECO:0000313|EMBL:ABQ03030.1};
RC PLASMID=pK29 {ECO:0000313|EMBL:ABQ03030.1};
RA Chen Y.-T., Wu K.-M., Liao T.-L., Shiau Y.-R., Yan J.-J., Su I.-J.,
RA Lauderdale T.-L., Tsai S.-F.;
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU361257};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594, ECO:0000256|RuleBase:RU361257}.
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DR EMBL; EF382672; ABQ03030.1; -; Genomic_DNA.
DR RefSeq; YP_001965973.1; NC_010870.1.
DR AlphaFoldDB; A7KGG3; -.
DR REBASE; 20259; M.KpnNK29ORF303P.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.1020.10; Adenine-specific Methyltransferase, Domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR012263; M_m6A_EcoRV.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00571; dam; 1.
DR PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR PANTHER; PTHR30481:SF3; 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.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU361257}; Plasmid {ECO:0000313|EMBL:ABQ03030.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU361257};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361257}.
SQ SEQUENCE 257 AA; 29303 MW; 888CDF3AD9EA5FFD CRC64;
MPFISHHYPH DHSCRWVEPF IGGGAVFLNM FAQNALLADS NPDLINLYRT IQRQKTNFIN
QVQNLADKTF VEKDYYEMRD RFNKTCISGQ PLQRAALFYS LNRLGYNGMC RYNSERIYSV
PWGKHTELKL DFNKIDYLSF RLSGIELITA GFEETLAATG EGDQIYCDPP YDKTSKTSFV
SYDGKPFSQS DHVLLANMLV DAHRKGAAVA ISNSLTPFTL GLYEERGFVI HRLSAYRSVG
SKPNTRKTET EILAVLK
//
