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MTTB_DESHD
ID   MTTB_DESHD              Reviewed;         496 AA.
AC   Q18TV3; Q18TV2;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Trimethylamine methyltransferase MttB;
DE            Short=TMA methyltransferase;
DE            EC=2.1.1.250;
DE   AltName: Full=Trimethylamine--corrinoid protein methyltransferase;
GN   OrderedLocusNames=Dhaf_4869;
OS   Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=272564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10664 / DCB-2;
RX   PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA   Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA   Tiedje J.M.;
RT   "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT   anaerobe capable of dehalogenation and metal reduction.";
RL   BMC Microbiol. 12:21-21(2012).
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   -!- SIMILARITY: Belongs to the trimethylamine methyltransferase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CP001336; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   OMA; ANITRFC; -.
DR   Proteomes; UP000007726; Chromosome.
DR   GO; GO:0043834; F:trimethylamine methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015948; P:methanogenesis; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.480; -; 1.
DR   InterPro; IPR038601; MttB-like_sf.
DR   InterPro; IPR010426; MTTB_MeTrfase.
DR   Pfam; PF06253; MTTB; 1.
DR   PIRSF; PIRSF037567; MTTB_MeTrfase; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Pyrrolysine; Transferase.
FT   CHAIN           1..496
FT                   /note="Trimethylamine methyltransferase MttB"
FT                   /id="PRO_0000249588"
FT   NON_STD         331
FT                   /note="Pyrrolysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   496 AA;  53572 MW;  531FE18109842B85 CRC64;
     MARLRSMVQA GVARVEGFGL AGFSDEELYA IHTSTLEVLE YTGLKIESQE ALEIFSEGGA
     RVDFKTKVVK IPQYLVEDAI QSAPSTLVLA GRNPKNDIVL GGKRVGFINF GEGVSIIDPY
     TKEYRKTTRR DVANITRFCD AMDQMDAVLR PVAPQDIHPS VAVVHNAEVI FNNTSKHVFI
     GVEGGRNFKK VLKMAAAVAG GEDKLRERPL FSCNICPTSP LQIVNHASEV IIEGARAGIP
     VNMLSMGMSG ATSAITLAGT LVTHNCEVLG AIVLSQLTSK GAPVLYGSST TIMDMKNMTA
     PVGSPELGMI NAGVAKLAQY YNLPSWVAGG OVDSKIPDAQ ASHEFTLTGF LTALAGANLI
     YGAGMLELGI TFDYAQMLMD NEMARMIKKA VGGISVTDET LAVDVIKSVG TAGNFISEDH
     TYAHMRTQSQ SKLVDRSMRE NWLAAGAKDF TQRAYEEAIS ILENYTPEPL PEKIAATLRS
     IVEETEDEYG VARSLI
 
 
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