ID   MTTB2_METMA             Reviewed;         495 AA.
AC   P58974;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   23-FEB-2022, entry version 98.
DE   RecName: Full=Trimethylamine methyltransferase MttB2;
DE            Short=TMA methyltransferase 2;
DE            EC=2.1.1.250;
DE   AltName: Full=Trimethylamine--corrinoid protein methyltransferase 2;
GN   Name=mttB2; OrderedLocusNames=MM_2048/MM_2049;
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 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   -!- SUBUNIT: Can form a complex with MttC. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the trimethylamine methyltransferase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM31744.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAM31745.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE008384; AAM31744.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AE008384; AAM31745.1; ALT_SEQ; Genomic_DNA.
DR   STRING; 192952.MM_2049; -.
DR   EnsemblBacteria; AAM31744; AAM31744; MM_2048.
DR   EnsemblBacteria; AAM31745; AAM31745; MM_2049.
DR   KEGG; mma:MM_2048; -.
DR   KEGG; mma:MM_2049; -.
DR   PATRIC; fig|192952.21.peg.2351; -.
DR   eggNOG; arCOG03406; Archaea.
DR   HOGENOM; CLU_149838_0_0_2; -.
DR   BRENDA; 2.1.1.250; 3270.
DR   UniPathway; UPA00645; -.
DR   Proteomes; UP000000595; 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..495
FT                   /note="Trimethylamine methyltransferase MttB2"
FT                   /id="PRO_0000216575"
FT   NON_STD         334
FT                   /note="Pyrrolysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   495 AA;  53910 MW;  993BEA3A5F98C9E6 CRC64;
     MAQNNAVAGF NALNGVELSL FTTDELKAIH YATMEVLMNP GVQVSDPEAR QIFKENGCEV
     DEKTSIVKIP EYLVRRALQL APSRFVLWGR DKKYNTVQEA GGKVHWTCFG TGVKMCKYQD
     GKYVTVDSVE QDIADIAKLC DWAENIDYFS LPVSARDWAG KGAQDVHETL TPIANTAKHY
     HHIDPVGEHV DYYRDIVKAY YGGDEEEARK KPIFSMLLCP TSPLELSVNA CQVIIRGARF
     GMPVNVLSMA MSGGSSPVYL AGTLVTHNAE VLSGIVLAQL TVPGAKVWYG SSTTTFDLKK
     GTAPVGSPEL GLISAAVAKL AQFYGLPSYV AGTOSDAKIP DNQAGHEKTM TCLLPALAGA
     NTIYGAGMLE LGMTFSMEQL VIDNDIIKMV KKAMQGIPVS PETLAVESIQ KVGIGNNFLA
     LKQTRMLVDY PSSPMLIDRR MFGDWAASGS KDLAAVANEK VQDILKNHQV PPVDADILKD
     MQAIVDKADR AFKEG