ID H6LJZ8_ACEWD Unreviewed; 932 AA.
AC H6LJZ8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=Awo_c19740 {ECO:0000313|EMBL:AFA48752.1};
OS Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655
OS / WB1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=931626 {ECO:0000313|EMBL:AFA48752.1, ECO:0000313|Proteomes:UP000007177};
RN [1] {ECO:0000313|Proteomes:UP000007177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC {ECO:0000313|Proteomes:UP000007177};
RA Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J.,
RA Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.;
RT "Complete genome sequence of Acetobacterium woodii.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFA48752.1, ECO:0000313|Proteomes:UP000007177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC {ECO:0000313|Proteomes:UP000007177};
RX PubMed=22479398; DOI=10.1371/journal.pone.0033439;
RA Poehlein A., Schmidt S., Kaster A.K., Goenrich M., Vollmers J., Thurmer A.,
RA Bertsch J., Schuchmann K., Voigt B., Hecker M., Daniel R., Thauer R.K.,
RA Gottschalk G., Muller V.;
RT "An ancient pathway combining carbon dioxide fixation with the generation
RT and utilization of a sodium ion gradient for ATP synthesis.";
RL PLoS ONE 7:E33439-E33439(2012).
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};
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DR EMBL; CP002987; AFA48752.1; -; Genomic_DNA.
DR RefSeq; WP_014356352.1; NC_016894.1.
DR AlphaFoldDB; H6LJZ8; -.
DR STRING; 931626.Awo_c19740; -.
DR REBASE; 45794; Awo1030IV.
DR KEGG; awo:Awo_c19740; -.
DR eggNOG; COG1002; Bacteria.
DR HOGENOM; CLU_005831_3_0_9; -.
DR OrthoDB; 9815272at2; -.
DR Proteomes; UP000007177; Chromosome.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR046818; MmeI_C.
DR InterPro; IPR046819; MmeI_hel.
DR InterPro; IPR046816; MmeI_Mtase.
DR InterPro; IPR046817; MmeI_N.
DR InterPro; IPR046820; MmeI_TRD.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR33841:SF6; DNA METHYLTRANSFERASE A; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR Pfam; PF20467; MmeI_C; 1.
DR Pfam; PF20465; MmeI_hel; 1.
DR Pfam; PF20473; MmeI_Mtase; 1.
DR Pfam; PF20464; MmeI_N; 1.
DR Pfam; PF20466; MmeI_TRD; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000007177};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..186
FT /note="MmeI-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF20464"
FT DOMAIN 199..273
FT /note="MmeI-like helicase spacer"
FT /evidence="ECO:0000259|Pfam:PF20465"
FT DOMAIN 361..625
FT /note="MmeI-like DNA-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF20473"
FT DOMAIN 643..844
FT /note="MmeI-like target recognition"
FT /evidence="ECO:0000259|Pfam:PF20466"
FT DOMAIN 846..925
FT /note="MmeI-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20467"
SQ SEQUENCE 932 AA; 106424 MW; CCC4EF97B5C5F058 CRC64;
MTDVEQRAAA KQFAEIWKDQ GYEKGQSQPF WLSLLRDIYG VKNPEQFIIF EDQVVLDHTS
FIDGIIPETH VLIEQKGINK DLRKAIKQSD GTMLSPFQQA KRYSADLPYS KRPRWIVTCN
FKAFLIYDME KPNGEPEEIL LENLPAETYR LEFLVDTGDS HIKKEMEISI QAGELVGELY
DELLKQYHQP DDPESLKCLN MLCVRLVFCL YAEDAGIFGK HGKFHSYLKD YDAKDVRRAL
IDLFAVLDTQ PADRDPYLEP TLASFPYVNG GLFSEKNIEI PNFNDTIVNL LLQNASEDFD
WSAISPTIFG AVFESTLNPA TRRSGGMHYT SIENIHKVID PLFLDELKEE FADIKAIAIE
KTRNRRLDDF QTKLSRLTFL DPACGSGNFL TESYLALRKL ENEVLKVLLG DQIRIGTDTH
TPIKVSINQF YGIEINDFAV SVGKTALWIA ESQMMMKTED IIHMHLDFLP LKTYANIIEG
NALKLDWETV VAKTSLDYIM GNPPFVGYSM QNDGQKKDIL AVYLDEQGKS YKTAGKIDFV
AGWYFKAAQL MDQTKIRTAF VSTNSITQGE QVAGVWKPLY ERFGIHIDFA YQTFKWASEA
KDKAAVHCVI VGFSQAYNAK EKYLYADVMI NQVTTINPYL VEAPVVFIEN IKKPICNVPE
MTTGNRPADG GHLLISDKDY DLFIEKEPKS KNYIKQFVGA AEFINNKKRW CLWLVNASPT
EIRSMPLVKE RVELCRIDRL NAPDAGRQKL AERPALFRET KNPKSYVSVP STSSENRRYI
PIGFLDDEYI PSNSTIILPD ATIYDFGILT SNVHMAWMRT VAGRLKSDYR YSINIVYNNF
IWPTPTDKQQ DMIEKTAQEI LNARALFPDS SFADLYDETV MPSALRKAHQ LNDRAVMDAY
GFDKKISESE CVAKLMRLYQ EKVTAVENKI TK
//
