MTBB3_METMA
ID MTBB3_METMA Reviewed; 467 AA.
AC P58972;
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=Dimethylamine methyltransferase MtbB3;
DE Short=DMA methyltransferase 3;
DE Short=DMAMT 3;
DE EC=2.1.1.249;
DE AltName: Full=Dimethylamine--corrinoid protein methyltransferase 3;
GN Name=mtbB3; OrderedLocusNames=MM_1693/MM_1694;
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 dimethylamine
CC to the corrinoid cofactor of MtbC. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Co(I)-[dimethylamine-specific corrinoid protein] +
CC dimethylamine + H(+) = methyl-Co(III)-[dimethylamine-specific
CC corrinoid protein] + methylamine; Xref=Rhea:RHEA:41175, Rhea:RHEA-
CC COMP:11122, Rhea:RHEA-COMP:11123, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58040, ChEBI:CHEBI:59338, ChEBI:CHEBI:85033,
CC ChEBI:CHEBI:85035; EC=2.1.1.249;
CC -!- PATHWAY: One-carbon metabolism; methanogenesis from dimethylamine.
CC -!- SIMILARITY: Belongs to the dimethylamine methyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM31389.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM31390.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE008384; AAM31389.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE008384; AAM31390.1; ALT_SEQ; Genomic_DNA.
DR STRING; 192952.MM_1693; -.
DR EnsemblBacteria; AAM31389; AAM31389; MM_1693.
DR EnsemblBacteria; AAM31390; AAM31390; MM_1694.
DR KEGG; mma:MM_1693; -.
DR KEGG; mma:MM_1694; -.
DR PATRIC; fig|192952.21.peg.1965; -.
DR eggNOG; arCOG06710; Archaea.
DR HOGENOM; CLU_046512_0_0_2; -.
DR UniPathway; UPA00644; -.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0043791; F:dimethylamine methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR InterPro; IPR012653; Dimeth_MeTrfase_MtbB.
DR Pfam; PF09505; Dimeth_Pyl; 1.
DR TIGRFAMs; TIGR02368; dimeth_PyL; 1.
PE 3: Inferred from homology;
KW Methanogenesis; Methyltransferase; Pyrrolysine; Reference proteome;
KW Transferase.
FT CHAIN 1..467
FT /note="Dimethylamine methyltransferase MtbB3"
FT /id="PRO_0000216568"
FT NON_STD 356
FT /note="Pyrrolysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 467 AA; 50469 MW; 3E9C29DB71021D5D CRC64;
MATEYALRMG DGKRIFLTKD KIIEELEAGM ANASDLGEIP DLSGDEIDKL AEILMMPGKA
VSVEQGMEVP VTHDIGTLRL DGDQGNSGVG IPSSRLVGCM MHERAFGADT MELGHIDYSY
KPVKPVVANE CQAMEVCQQN MIIPLFYGAM PNMGLYYTPD GPFENPGDLM KAFKIQEAWD
SMEHAAAHLT RDTVWVMQKL FASGADGVNF DTTAAAGDAD MYGTLHAIEA LRKEFPDMYI
EAGMAGECVL GMHGNLQYDG VTLAGLWPHQ QAPLIAKAGA NVFGPVCNTN TSKTSPWNLA
RAVNFMKAAV QASSIPCHVD MGMGVGGIPM LETPPIDAVT RASKAMVEIA GVDGIOIGVG
DPLGMPISHI MASGMTGMRA AGDLVARMQF SKNMKIKEAK EYVAKKLNVE TMDLADEYVM
RELREELDIG VITSVPGAAK GIAAKMNIEK LLDVKINSCN LFRKQTR
