MTBB1_METBF
ID MTBB1_METBF Reviewed; 467 AA.
AC P0C0W5;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Dimethylamine methyltransferase MtbB1;
DE Short=DMA methyltransferase 1;
DE Short=DMAMT 1;
DE EC=2.1.1.249;
DE AltName: Full=Dimethylamine--corrinoid protein methyltransferase 1;
GN Name=mtbB1; OrderedLocusNames=Mbar_A1506;
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 MtbB1"
FT /id="PRO_0000216561"
FT NON_STD 356
FT /note="Pyrrolysine"
FT /evidence="ECO:0000250"
FT CONFLICT 16
FT /note="Y -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 467 AA; 50311 MW; AD08B1C0AF6F1BDF CRC64;
MATEYALRMG DGKRIYLTKE KIIAEIEDGT ANAADLGEIP ALNANEMEKL AEILMMPGKT
VSVEQGMEVP VTHDIGTIRL DGDQGNSGVG IPSSRLVGCM THERAFGADT MELGHIDYSF
KPVKPVVSNE CQAMEVCQQN MIIPLFYGAM PNMGLYYTPD GPFENPGDLM KAFKIPEAWE
SMEHAAEHLT RDTVWVMQKL FASGADGVNF DTTGAAGDGD MYGTLHAIEA LRKEFPDMYI
EAGMAGECVL GMHGNLQYDG VTLAGLWPHQ QAPLVAKAGA NVFGPVCNTN TSKTSAWNLA
RAVTFMKAAV EASPIPCHVD MGMGVGGIPM LETPPIDAVT RASKAMVEIA GVDGIOIGVG
DPMGMPIAHI MASGMTGMRA AGDLVARMEF SKNMRIGEAK EYVAKKLGVD QMDLVDEHVM
RELREELDIG IITSVPGAAK GIAAKMNIEK LLDIKINSCN LFRKQIA