ID   MTTB_METBA              Reviewed;         495 AA.
AC   O93658;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 4.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Trimethylamine methyltransferase MttB;
DE            Short=TMA methyltransferase;
DE            EC=2.1.1.250 {ECO:0000269|PubMed:9006042};
DE   AltName: Full=Trimethylamine--corrinoid protein methyltransferase;
GN   Name=mttB {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 2-18, PATHWAY, AND
RP   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   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX   PubMed=9006042; DOI=10.1128/jb.179.3.846-852.1997;
RA   Ferguson D.J. Jr., Krzycki J.A.;
RT   "Reconstitution of trimethylamine-dependent coenzyme M methylation with the
RT   trimethylamine corrinoid protein and the isozymes of methyltransferase II
RT   from Methanosarcina barkeri.";
RL   J. Bacteriol. 179:846-852(1997).
RN   [3]
RP   PYRROLYSINE AT PYL-334.
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 trimethylamine
CC       to the corrinoid cofactor of MttC. {ECO:0000269|PubMed:9006042}.
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         Evidence={ECO:0000269|PubMed:9006042};
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from trimethylamine.
CC       {ECO:0000305|PubMed:10762254}.
CC   -!- SUBUNIT: Can form a complex with MttC.
CC   -!- INDUCTION: Induced by growth on trimethylamine but not methanol or
CC       monomethylamine. Part of the mtbC-mttB-mttC and mtbC-mttB-mttC-mttP-
CC       mtbB1 operons. {ECO:0000269|PubMed:10762254}.
CC   -!- SIMILARITY: Belongs to the trimethylamine methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AF102623; AAD14630.2; -; Genomic_DNA.
DR   KEGG; ag:AAD14630; -.
DR   BioCyc; MetaCyc:MON-12208; -.
DR   BRENDA; 2.1.1.250; 3250.
DR   UniPathway; UPA00645; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Methanogenesis; Methyltransferase; Pyrrolysine;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10762254"
FT   CHAIN           2..495
FT                   /note="Trimethylamine methyltransferase MttB"
FT                   /id="PRO_0000216569"
FT   NON_STD         334
FT                   /note="Pyrrolysine"
FT                   /evidence="ECO:0000269|PubMed:16096277"
SQ   SEQUENCE   495 AA;  53855 MW;  A328C3039F06B81B CRC64;
     MAKNNAVAGF NALNGVELNL FTTDELKAIH YATMEVLMDP GIQVSDPEAR QIFKENGCEV
     NEKTNVVKIP EYLVRKALQL APSRFVLWGR DKKFNTVQEC GGKVHWTCFG TGVKVCKYQD
     GKYVTVDSVE KDIADIAKLC DWAENIDYFS LPVSARDIAG QGAQDVHETL TPLANTAKHF
     HHIDPVGENV EYYRDIVKAY YGGDEEEARK KPIFSMLLCP TSPLELSVNA CQVIIKGARF
     GIPVNVLSMA MSGGSSPVYL AGTLVTHNAE VLSGIVLAQL TVPGAKVWYG SSTTTFDLKK
     GTAPVGSPEL GLISAAVAKL AQFYGLPSYV AGSOSDAKVP DDQAGHEKTM TTLLPALAGA
     NTIYGAGMLE LGMTFSMEQL VIDNDIFSMV KKAMQGIPVS EETLAVESIQ KVGIGNNFLA
     LKQTRQLVDY PSNPMLLDRH MFGDWAAAGS KDLATVAHEK VEDVLKNHQV TPIDADIFKD
     MQAIVDKADK AFRGM