ID   MTTB2_METAC             Reviewed;         495 AA.
AC   Q8TS73;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   23-FEB-2022, entry version 86.
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=MA_0932;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(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}.
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DR   EMBL; AE010299; AAM04365.1; -; Genomic_DNA.
DR   STRING; 188937.MA_0932; -.
DR   PRIDE; Q8TS73; -.
DR   KEGG; mac:MA_0932; -.
DR   HOGENOM; CLU_033581_1_0_2; -.
DR   InParanoid; Q8TS73; -.
DR   OMA; NQACIIS; -.
DR   UniPathway; UPA00645; -.
DR   Proteomes; UP000002487; 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_0000216573"
FT   NON_STD         334
FT                   /note="Pyrrolysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   495 AA;  54078 MW;  7C8A0AC95D5E24D6 CRC64;
     MAQNNAVAGF SSLQGVELNL FTIDELKAIH YATMEVLMNP GVQVSDPEAR QIFKENGCEV
     DEKTNVVKIP EYLVRRALQL APSRFVLWGR DKKYNTVQEA GGKVHWTCFG TGVKMCKYQS
     GKYVTVDSVE QDIADIAKLC DWTENIDYFS LPVSARDWAG KGAQDVHETL TPIANTAKHY
     HHIDPVGENV EYYRDIVKAY YGGDEEEARK KPIFSMLLCP TSPLELSVNA CQVIIKGARF
     GMPVNVLSMA MSGGSSPVYL AGTLVTHNAE VLSGIVLAQL TVPGAKVWYG SSTTTFDLKK
     GTAPVGSPEL GLISAAVAKL AQFYGLPSYV AGTOADAKIP DNQTGHEKTM TCFLPALAGA
     NTIYGAGMLE LGMTFSMEQL VIDNDIIKMV KKAMQGIEVS PETLAVDSIQ KVGIGNNFLA
     LKQTRLLVNY PSDPMLIDRR MYGDWAASGS KDLAAVANEK VTDVLKHHEV PPIDTDILKD
     MQAIVDRADK AFKES