ID   MTBB2_METMA             Reviewed;         467 AA.
AC   P58971;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   23-FEB-2022, entry version 101.
DE   RecName: Full=Dimethylamine methyltransferase MtbB2;
DE            Short=DMA methyltransferase 2;
DE            Short=DMAMT 2;
DE            EC=2.1.1.249;
DE   AltName: Full=Dimethylamine--corrinoid protein methyltransferase 2;
GN   Name=mtbB2; OrderedLocusNames=MM_2962/MM_2963;
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=AAM32658.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAM32659.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE008384; AAM32658.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AE008384; AAM32659.1; ALT_SEQ; Genomic_DNA.
DR   STRING; 192952.MM_2962; -.
DR   EnsemblBacteria; AAM32658; AAM32658; MM_2962.
DR   EnsemblBacteria; AAM32659; AAM32659; MM_2963.
DR   KEGG; mma:MM_2962; -.
DR   KEGG; mma:MM_2963; -.
DR   PATRIC; fig|192952.21.peg.3438; -.
DR   eggNOG; arCOG06710; Archaea.
DR   HOGENOM; CLU_046512_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..467
FT                   /note="Dimethylamine methyltransferase MtbB2"
FT                   /id="PRO_0000216567"
FT   NON_STD         356
FT                   /note="Pyrrolysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   467 AA;  50517 MW;  1A69899E455D7A3E CRC64;
     MATEYALRMG DGKRIFLTKD KIMEELEAGM ANASDLGEIP DLSGDEIDKL AEILMMPGKT
     VSVEQGMEVP VTHDIGTLRL DGDQGNSGVG IPSSRLVGCM MHERAFGADT MELGHIDYSY
     KPVKPVVANE CQAMEVCQQN MIIPLFYGAM PNMGLYYTPD GPFENPGDLM KAFKIQEAWD
     SMEHAAAHLT RDTVWVMQKL FASGADGVNF DTTAAAGDAD MYGTLHAIEA LRKEFPDMYI
     EAGMAGECVL GMHGNLQYDG VTLAGLWPHQ QAPLIAKAGA NVFGPVCNTN TSKTSPWNLA
     RAVNFMKAAV QASSIPCHVD MGMGVGGIPM LETPPIDAVT RASKAMVEIA GVDGIOIGVG
     DPLGMPISHI MASGMTGMRA AGDLVARMQF SKNMKIKEAK EYVAKKLNVE TMDLADEYVM
     RELREELDIG VITSVPGAAK GIAAKMNIEK LLDVKINSCN LFRKQTR