ID   MTBB2_METBA             Reviewed;         419 AA.
AC   Q9P9N0;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   23-FEB-2022, entry version 50.
DE   RecName: Full=Dimethylamine methyltransferase MtbB2;
DE            Short=DMA methyltransferase 2;
DE            Short=DMAMT 2;
DE            EC=2.1.1.249 {ECO:0000250|UniProtKB:O93661};
DE   AltName: Full=Dimethylamine--corrinoid protein methyltransferase 2;
DE   Flags: Fragment;
GN   Name=mtbB2 {ECO:0000303|PubMed:10762254};
OS   Methanosarcina barkeri.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2208;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC   STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX   PubMed=10762254; DOI=10.1128/jb.182.9.2520-2529.2000;
RA   Paul L., Ferguson D.J. Jr., Krzycki J.A.;
RT   "The trimethylamine methyltransferase gene and multiple dimethylamine
RT   methyltransferase genes of Methanosarcina barkeri contain in-frame and
RT   read-through amber codons.";
RL   J. Bacteriol. 182:2520-2529(2000).
RN   [2]
RP   NO DETECTED EXPRESSION.
RC   STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX   PubMed=16096277; DOI=10.1074/jbc.m506402200;
RA   Soares J.A., Zhang L., Pitsch R.L., Kleinholz N.M., Jones R.B., Wolff J.J.,
RA   Amster J., Green-Church K.B., Krzycki J.A.;
RT   "The residue mass of L-pyrrolysine in three distinct methylamine
RT   methyltransferases.";
RL   J. Biol. Chem. 280:36962-36969(2005).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from dimethylamine
CC       to the corrinoid cofactor of MtbC (By similarity). No evidence for
CC       expression of this protein has been found after growth under presumably
CC       inducing conditions (PubMed:16096277). {ECO:0000250,
CC       ECO:0000250|UniProtKB:O93661, ECO:0000269|PubMed:16096277}.
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         Evidence={ECO:0000250|UniProtKB:O93661};
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from dimethylamine.
CC       {ECO:0000305|PubMed:10762254}.
CC   -!- SIMILARITY: Belongs to the dimethylamine methyltransferase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF153453; AAD38790.2; -; Genomic_DNA.
DR   BRENDA; 2.1.1.249; 3250.
DR   UniPathway; UPA00644; -.
DR   GO; GO:0043791; F:dimethylamine methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:2001129; P:methane biosynthetic process from dimethylamine; ISS:UniProtKB.
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; Transferase.
FT   CHAIN           <1..419
FT                   /note="Dimethylamine methyltransferase MtbB2"
FT                   /id="PRO_0000216559"
FT   NON_STD         308
FT                   /note="Pyrrolysine"
FT                   /evidence="ECO:0000250|UniProtKB:O93661"
FT   NON_TER         1
SQ   SEQUENCE   419 AA;  44985 MW;  F83666BB81947FDE CRC64;
     KLAEILMMPG KTVSVEQGME IPVTHDIGTI RLDGDQGNSG VGIPSSRLVG CMTHERAFGA
     DTMELGHIDY SFKPVKPVVS NECQAMEVCQ QNMVIPLFYG AMPNMGLYYT PDGPFENPGD
     LMKAFKIQEA WESMEHAAEH LTRDTVWVMQ KLFASGADGV NFDTTGAAGD GDMYGTLHAI
     EALRKEFPDM YIEAGMAGEC VLGMHGNLQY DGVTLAGLWP HQQAPLVAKA GANVFGPVCN
     TNTSKTSAWN LARAVTFIKA AVGASPIPCH VNMGMGVGGI PMLETPPIDA VTRASKAMVE
     IAGVDGIOIG VGDPMGMPIS HIMASGMTGM RAAGDLVARM EFSKNMRIGE AKEYVAKKLG
     VDKMDLVDEH VMRELREELD IGIITSVPGA AKGIAAKMNI EKLLGIKINS CNLFRKQIA