MTTB_DESHY
ID MTTB_DESHY Reviewed; 496 AA.
AC Q24MI3; Q24MI4;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-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 OrderedLocusNames=DSY4970/DSY4969;
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=138119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y51;
RX PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT "Complete genome sequence of the dehalorespiring bacterium
RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT ethenogenes 195.";
RL J. Bacteriol. 188:2262-2274(2006).
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=BAE86758.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE86759.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP008230; BAE86759.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008230; BAE86758.1; ALT_SEQ; Genomic_DNA.
DR STRING; 138119.DSY4970; -.
DR EnsemblBacteria; BAE86758; BAE86758; DSY4969.
DR EnsemblBacteria; BAE86759; BAE86759; DSY4970.
DR KEGG; dsy:DSY4969; -.
DR KEGG; dsy:DSY4970; -.
DR eggNOG; COG5598; Bacteria.
DR HOGENOM; CLU_149838_0_0_9; -.
DR Proteomes; UP000001946; 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; Reference proteome; Transferase.
FT CHAIN 1..496
FT /note="Trimethylamine methyltransferase MttB"
FT /id="PRO_0000249589"
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
