MTBB3_METBA
ID MTBB3_METBA Reviewed; 419 AA.
AC Q9P9M9;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 23-FEB-2022, entry version 51.
DE RecName: Full=Dimethylamine methyltransferase MtbB3;
DE Short=DMA methyltransferase 3;
DE Short=DMAMT 3;
DE EC=2.1.1.249 {ECO:0000250|UniProtKB:O93661};
DE AltName: Full=Dimethylamine--corrinoid protein methyltransferase 3;
DE Flags: Fragment;
GN Name=mtbB3 {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], AND PATHWAY.
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 NO DETECTED EXPRESSION.
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 dimethylamine
CC to the corrinoid cofactor of MtbC (By similarity). No evidence for
CC expression of this protein has been found after growth under presumably
CC inducing conditions (PubMed:16096277). {ECO:0000250,
CC ECO:0000250|UniProtKB:O93661, ECO:0000269|PubMed:16096277}.
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:0000250|UniProtKB:O93661};
CC -!- PATHWAY: One-carbon metabolism; methanogenesis from dimethylamine.
CC {ECO:0000305|PubMed:10762254}.
CC -!- SIMILARITY: Belongs to the dimethylamine methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF153454; AAD38791.2; -; Genomic_DNA.
DR BRENDA; 2.1.1.249; 3250.
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 3: Inferred from homology;
KW Methanogenesis; Methyltransferase; Pyrrolysine; Transferase.
FT CHAIN <1..419
FT /note="Dimethylamine methyltransferase MtbB3"
FT /id="PRO_0000216560"
FT NON_STD 308
FT /note="Pyrrolysine"
FT /evidence="ECO:0000250|UniProtKB:O93661"
FT NON_TER 1
SQ SEQUENCE 419 AA; 45051 MW; 3488DC1C4675E7E4 CRC64;
KLAEILMMPG KTVSVEQGME IPVTHDIGTI RLDGDQGNSG VGIPSSRLVG CMTHERAFGA
DTMELGHIDY SFKPVKPVVS NECQAMEVCQ QNMVIPLFYG AMPNMGLYYT PDGPFENPGD
LMKLFKIDKA KESMEHAAEH LTRDTVWVMQ KLFASGADGV NFDTTGAAGD GDMYGTLYAI
QALRKEFSDM YIEAGMAGEM VLGMHGELEY NGVRLAGLWP HEQAPLVAKA GANVFGPVCN
TNTSKTSAWN LARAVTFIKA AVGASPIPCH VNMGMGVGGI PMLETPPIDA VTRASKAMVE
IAGVDGIOIG VGDPMGMPIS HIMASGMTGI RAAGDLVARM EFSKNMRIGE AKEYVAKKLG
VDKMDLVDEH VMRELREELD IGIITSVPGA AKGIAAKMNI EKLLGIKINS CNLFRKQIA
