ID   MTBB2_METBF             Reviewed;         467 AA.
AC   P0C0W6;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Dimethylamine methyltransferase MtbB2;
DE            Short=DMA methyltransferase 2;
DE            Short=DMAMT 2;
DE            EC=2.1.1.249;
DE   AltName: Full=Dimethylamine--corrinoid protein methyltransferase 2;
GN   Name=mtbB2; OrderedLocusNames=Mbar_A3605;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-17, FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=9654067; DOI=10.1046/j.1432-1327.1998.2530692.x;
RA   Wassenaar R.W., Keltjens J.T., van der Drift C., Vogels G.D.;
RT   "Purification and characterization of dimethylamine:5-
RT   hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri
RT   Fusaro.";
RL   Eur. J. Biochem. 253:692-697(1998).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from dimethylamine
CC       to the corrinoid cofactor of MtbC. {ECO:0000269|PubMed:9654067}.
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         Evidence={ECO:0000269|PubMed:9654067};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.45 mM for dimethylamine {ECO:0000269|PubMed:9654067};
CC         KM=4.5 mM for monomethylamine {ECO:0000269|PubMed:9654067};
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from dimethylamine.
CC   -!- SIMILARITY: Belongs to the dimethylamine methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   UniPathway; UPA00644; -.
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   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:9654067"
FT   CHAIN           2..467
FT                   /note="Dimethylamine methyltransferase MtbB2"
FT                   /id="PRO_0000216562"
FT   NON_STD         356
FT                   /note="Pyrrolysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        15..16
FT                   /note="VF -> IK (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   467 AA;  50408 MW;  D2E76FCDFB8C9EDB CRC64;
     MATEYALRMG DGKRVFLTKE KIMAEIEAGT ANAADLGDIP ALNDNEMDKL AEILMMPGKT
     VSVEQGMEIP VTHDIGTIRL DGDQGNSGVG IPSSRLVGCM MHERAFGADT MELGHIDYSF
     KPVKPVVSNE CQAMEVCQQN MIIPLFYGAM PNMGLYYTPD GPFENPGDLM KLFKIDKAKE
     SMEHAAEHLT RDTVWVMQKL FASGADGVNF DTTGAAGDGD MYGTLYAIQA LRKEFPDMYI
     EAGMAGEMVL GMHGELEYDG VRLAGSWPHE QAPLIAKAGA NVFGPVCNTN TSKTSAWNLA
     RAVTFIKAAV EASPIPCHVN MGMGVGGIPM LETPPIDAVT RASKAMVEIA GVDGIOIGVG
     DPMGMPISHI MASGMTGIRA AGDLVARMEF SKNMRIGEAK EYVAKKLGVD KMDLVDEHVM
     RELREELDIG IITSVPGAAK GIAAKMNIEK LLDIKINSCN LFRKQIA