ID A2SNH6_METPP Unreviewed; 473 AA.
AC A2SNH6;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=C-5 cytosine-specific DNA methylase {ECO:0000313|EMBL:ABM97115.1};
GN OrderedLocusNames=Mpe_B0340 {ECO:0000313|EMBL:ABM97115.1};
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OG Plasmid RPME01 {ECO:0000313|EMBL:ABM97115.1,
OG ECO:0000313|Proteomes:UP000000366}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM97115.1, ECO:0000313|Proteomes:UP000000366};
RN [1] {ECO:0000313|EMBL:ABM97115.1, ECO:0000313|Proteomes:UP000000366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC {ECO:0000313|Proteomes:UP000000366};
RC PLASMID=RPME01 {ECO:0000313|EMBL:ABM97115.1,
RC ECO:0000313|Proteomes:UP000000366};
RX PubMed=17158667; DOI=10.1128/JB.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC Evidence={ECO:0000256|ARBA:ARBA00000743};
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01016}.
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DR EMBL; CP000556; ABM97115.1; -; Genomic_DNA.
DR RefSeq; WP_011831703.1; NC_008826.1.
DR AlphaFoldDB; A2SNH6; -.
DR REBASE; 14695; M.MpePMORF340P.
DR KEGG; mpt:Mpe_B0340; -.
DR eggNOG; COG0270; Bacteria.
DR HOGENOM; CLU_030951_0_0_4; -.
DR Proteomes; UP000000366; Plasmid RPME01.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF00145; DNA_methylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01016}; Plasmid {ECO:0000313|EMBL:ABM97115.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000366};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU01016};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01016}.
FT ACT_SITE 214
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 473 AA; 52054 MW; 6979C36ED4F959AF CRC64;
MTSLHTYAVR KIGSHRGSPR LWLEGREPTK GGFLPGTRFN TRVDTGRALL VLEAVEDGVR
IVSGKQRGDR QIPVIDINSK ELLDIFTGIE AVRVIVQEGV ISILPLASEL RARERVIRLK
DGLANGTLST GSVSSGIGVL DRAAHEGLEQ AGVECRLAFA NEIREDCVEH MCDHNPIVDQ
HTVTLTAPMQ ELAFDEWAMS RLPKVDVLVG GIPCSGASRA GRAKRGASHA EAHPEVGHLI
VAFLAIIAKV NPSAIVLENV PVWGTSASMF ILRNQLRDLG YDVHETIVNS AEWNVLEHRE
RLCVVAVTKG IEFSFDGLER PEPVSRRLGE IMDEVPVDAP CWSEMAYLKD KRARDEAKGN
NFKMTVLTPD SEKVPCLNKS LWKRQSSGSF WKHPDDSNLL RLPTVREHAR CKGVWEDLVE
GVGLTFGHEA LGQSVTVPPF ISIFKLLGQA LKRFASEAEA SIQPFALREL KAA
//
