ID   MTBB1_METBA             Reviewed;         467 AA.
AC   O93661; Q9C4B8;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Dimethylamine methyltransferase MtbB1;
DE            Short=DMA methyltransferase 1;
DE            Short=DMAMT 1;
DE            EC=2.1.1.249 {ECO:0000269|PubMed:10852929};
DE   AltName: Full=Dimethylamine--corrinoid protein methyltransferase 1;
GN   Name=mtbB1 {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], PROTEIN SEQUENCE OF 1-20 AND 460-467,
RP   PATHWAY, AND INDUCTION BY TRIMETHYLAMINE.
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   PROTEIN SEQUENCE OF 1-20, FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX   PubMed=10852929; DOI=10.1074/jbc.m910218199;
RA   Ferguson D.J. Jr., Gorlatova N., Grahame D.A., Krzycki J.A.;
RT   "Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete
RT   corrinoid protein and two methyltransferases purified from Methanosarcina
RT   barkeri.";
RL   J. Biol. Chem. 275:29053-29060(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-467.
RA   Srinivasan G., Paul L., Lienard T., Gottschalk G., Krzycki J.A.;
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PYRROLYSINE AT PYL-356.
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 (PubMed:10852929). The major or
CC       perhaps only DMA methyltransferase expressed under inducing conditions
CC       (PubMed:16096277). {ECO:0000269|PubMed:10852929,
CC       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:0000269|PubMed:10852929};
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from dimethylamine.
CC       {ECO:0000305|PubMed:10762254}.
CC   -!- SUBUNIT: May form homotetramers or homopentamers.
CC   -!- INDUCTION: Induced by growth on trimethylamine but not methanol or
CC       monomethylamine. Part of the mtbC-mttB-mttC-mttP-mtbB1 operon.
CC       {ECO:0000269|PubMed:10762254}.
CC   -!- SIMILARITY: Belongs to the dimethylamine methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AF102623; AAD14633.2; -; Genomic_DNA.
DR   EMBL; AF337056; AAK29407.1; -; Genomic_DNA.
DR   KEGG; ag:AAD14633; -.
DR   BioCyc; MetaCyc:MON-12212; -.
DR   BRENDA; 2.1.1.249; 3250.
DR   UniPathway; UPA00644; -.
DR   GO; GO:0043791; F:dimethylamine methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:2001129; P:methane biosynthetic process from dimethylamine; IDA: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   1: Evidence at protein level;
KW   Direct protein sequencing; Methanogenesis; Methyltransferase; Pyrrolysine;
KW   Transferase.
FT   CHAIN           1..467
FT                   /note="Dimethylamine methyltransferase MtbB1"
FT                   /id="PRO_0000216558"
FT   NON_STD         356
FT                   /note="Pyrrolysine"
FT                   /evidence="ECO:0000269|PubMed:16096277"
SQ   SEQUENCE   467 AA;  50228 MW;  A865C10BF8E252BA CRC64;
     MATEYALRMG DGKRVYLTKE KIVSEIEAGT ADAADLGEIP ALSANEMDKL AEILMMPGKT
     VSVEQGMEIP VTHDIGTIRL DGDQGNSGVG IPSSRLVGCM THERAFGADT MELGHIDYSF
     KPVKPVVSNE CQAMEVCQQN MVIPLFYGAM PNMGLYYTPD GPFENPGDLM KAFKIQEAWE
     SMEHAAEHLT RDTVWVMQKL FASGADGVNF DTTGAAGDGD MYGTLHAIEA LRKEFPDMYI
     EAGMAGECVL GMHGNLQYDG VTLAGLWPHQ QAPLVAKAGA NVFGPVCNTN TSKTSAWNLA
     RAVTFMKAAV EASPIPCHVD MGMGVGGIPM LETPPIDAVT RASKAMVEIA GVDGIOIGVG
     DPLGMPIAHI MASGMTGMRA AGDLVARMEF SKNMRIGEAK EYVAKKLGVD KMDLVDEHVM
     RELREELDIG IITSVPGAAK GIAAKMNIEK LLDIKINSCN LFRKQIA