ID   MTTB_METBU              Reviewed;         497 AA.
AC   Q12TR2; Q12TR1;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   23-FEB-2022, entry version 69.
DE   RecName: Full=Trimethylamine methyltransferase MttB;
DE            Short=TMA methyltransferase;
DE            EC=2.1.1.250;
DE   AltName: Full=Trimethylamine--corrinoid protein methyltransferase;
GN   Name=mttB; OrderedLocusNames=Mbur_2308; ORFNames=Mbur_2309;
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA   Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA   Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA   Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(2009).
RN   [2]
RP   SEQUENCE REVISION.
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Kadner K.,
RA   Aerts A., Dehal P., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Anderson I., Franzmann P., Thomas T.,
RA   Saunders N., Cavicchioli R., Sowers K., Richardson P.;
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from trimethylamine
CC       to the corrinoid cofactor of MttC. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Co(I)-[trimethylamine-specific corrinoid protein] + H(+) +
CC         trimethylamine = dimethylamine + methyl-Co(III)-[trimethylamine-
CC         specific corrinoid protein]; Xref=Rhea:RHEA:39287, Rhea:RHEA-
CC         COMP:11124, Rhea:RHEA-COMP:11126, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58040, ChEBI:CHEBI:58389, ChEBI:CHEBI:85033,
CC         ChEBI:CHEBI:85035; EC=2.1.1.250;
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from trimethylamine.
CC   -!- SIMILARITY: Belongs to the trimethylamine methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000300; ABE53164.2; -; Genomic_DNA.
DR   STRING; 259564.Mbur_2308; -.
DR   KEGG; mbu:Mbur_2308; -.
DR   HOGENOM; CLU_033581_1_0_2; -.
DR   UniPathway; UPA00645; -.
DR   Proteomes; UP000001979; Chromosome.
DR   GO; GO:0043834; F:trimethylamine methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.480; -; 1.
DR   InterPro; IPR038601; MttB-like_sf.
DR   InterPro; IPR012740; MttB_Methanosar.
DR   InterPro; IPR010426; MTTB_MeTrfase.
DR   Pfam; PF06253; MTTB; 1.
DR   PIRSF; PIRSF037567; MTTB_MeTrfase; 1.
DR   TIGRFAMs; TIGR02369; trimeth_pyl; 1.
PE   3: Inferred from homology;
KW   Methanogenesis; Methyltransferase; Pyrrolysine; Reference proteome;
KW   Transferase.
FT   CHAIN           1..497
FT                   /note="Trimethylamine methyltransferase MttB"
FT                   /id="PRO_0000249587"
FT   NON_STD         335
FT                   /note="Pyrrolysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   497 AA;  53950 MW;  50EF22AFC0617C8E CRC64;
     MTNENLCAGR NRYDGVSIDF FSDADLRAID SATMDVFQNP GIQVSDAESR ALFKEAGCDV
     NEKTMVVKIP EHVVRRAIMT APSKITLYGR EKQHTFTQQA GGKVHYTCFG TGVKMCKYEA
     PGVFKTVDST EEDLANTARV CDWADNIDSY SLAVSARDWA GKGAQDVHET FTPLMNTSKH
     FFHIDPVGEN VEYYWDILKA YYGGDEEQAR SRPIFSELLC PTSPLKIGTN ACQLILKSVN
     FGIPINVISM AMSGASCPVH LAGTLVTHNA EVLSGIVLAQ LASPGAKVWY GSSTTAFDLK
     HGTAPVGSPE LGLISAAVAK LGQYYDLPTY VASTOTDAKV PDGQAGHEKT LTNLLPALAG
     ANTLYGAGML ELGMTFSMEQ LMIDNDIISM GKKVMKGIPV NDETLGLASI QKVGIGNNFL
     AHKETRDNIN LVSSPDIFDR DMFGDWAAAG SKDIATVAHE KVTEILKNHE VTPIDSDLVR
     DMKAVVDRAD ADFRSSM