ID   MTBB1_METMA             Reviewed;         468 AA.
AC   P58970;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   23-FEB-2022, entry version 97.
DE   RecName: Full=Dimethylamine methyltransferase MtbB1;
DE            Short=DMA methyltransferase 1;
DE            Short=DMAMT 1;
DE            EC=2.1.1.249;
DE   AltName: Full=Dimethylamine--corrinoid protein methyltransferase 1;
GN   Name=mtbB1; OrderedLocusNames=MM_2050/MM_2051;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from dimethylamine
CC       to the corrinoid cofactor of MtbC. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Co(I)-[dimethylamine-specific corrinoid protein] +
CC         dimethylamine + H(+) = methyl-Co(III)-[dimethylamine-specific
CC         corrinoid protein] + methylamine; Xref=Rhea:RHEA:41175, Rhea:RHEA-
CC         COMP:11122, Rhea:RHEA-COMP:11123, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58040, ChEBI:CHEBI:59338, ChEBI:CHEBI:85033,
CC         ChEBI:CHEBI:85035; EC=2.1.1.249;
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from dimethylamine.
CC   -!- SIMILARITY: Belongs to the dimethylamine methyltransferase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM31746.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAM31747.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE008384; AAM31746.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AE008384; AAM31747.1; ALT_SEQ; Genomic_DNA.
DR   STRING; 192952.MM_2051; -.
DR   EnsemblBacteria; AAM31746; AAM31746; MM_2050.
DR   EnsemblBacteria; AAM31747; AAM31747; MM_2051.
DR   KEGG; mma:MM_2050; -.
DR   KEGG; mma:MM_2051; -.
DR   PATRIC; fig|192952.21.peg.2354; -.
DR   eggNOG; arCOG06710; Archaea.
DR   HOGENOM; CLU_2257397_0_0_2; -.
DR   UniPathway; UPA00644; -.
DR   Proteomes; UP000000595; Chromosome.
DR   GO; GO:0043791; F:dimethylamine methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   InterPro; IPR012653; Dimeth_MeTrfase_MtbB.
DR   Pfam; PF09505; Dimeth_Pyl; 1.
DR   TIGRFAMs; TIGR02368; dimeth_PyL; 1.
PE   3: Inferred from homology;
KW   Methanogenesis; Methyltransferase; Pyrrolysine; Reference proteome;
KW   Transferase.
FT   CHAIN           1..468
FT                   /note="Dimethylamine methyltransferase MtbB1"
FT                   /id="PRO_0000216566"
FT   NON_STD         356
FT                   /note="Pyrrolysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   468 AA;  50667 MW;  2380479541A61A4A CRC64;
     MATEYALRMG DGKRVFLARE KIMEEIEAGT ANAADLGEIP ALSADEMNKL AEILMMPGKA
     VSVEHGMEIP VTHDIGTIRL DGDQGNSGVG IPSSRLVGCM MHERAFGADT MELGHIDYSF
     KPVKPVVANE CQAMEVCQQN MIIPLFYGAM PNMGLYYTPD GPFENPGDLM KAFKIQEAWD
     SMEHAAEHLT RDTIWIMQKL FASGADGVNF DTTAAAGDGD FYGTLHAIEA LRKEFPEMYI
     EAGMAGEMVL GMHGNLQYDG VTLAGLWPHQ QAPLVAKAGA NVFGPVVNTN TSKTSPWNLA
     RAVTFIKEAV KVSSLPCHVD MGMGVGGIPM LETPPIDAVT RASKAMVEIA GVDGIOIGVG
     DPLGMPISHI MASGMTGMRA AGDLVARMQF SKNMKIKEAK EYVAKKLNVE IRDLADEYIM
     RELREELNIG VITSVPGSAK GIAAKMNIEK LLGIKINSCE LFRKQTGK