MTMB_METMA
ID MTMB_METMA Reviewed; 458 AA.
AC P58969;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 23-FEB-2022, entry version 104.
DE RecName: Full=Monomethylamine methyltransferase MtmB;
DE Short=MMA methyltransferase;
DE Short=MMAMT;
DE EC=2.1.1.248;
GN Name=mtmB1; OrderedLocusNames=MM_1436/MM_1437;
GN and
GN Name=mtmB2; OrderedLocusNames=MM_3335/MM_3336;
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 the methyl group from
CC monomethylamine to the corrinoid cofactor of MtmC. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Co(I)-[methylamine-specific corrinoid protein] + H(+) +
CC methylamine = methyl-Co(III)-[methylamine-specific corrinoid protein]
CC + NH4(+); Xref=Rhea:RHEA:26059, Rhea:RHEA-COMP:11120, Rhea:RHEA-
CC COMP:11121, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:59338,
CC ChEBI:CHEBI:85033, ChEBI:CHEBI:85035; EC=2.1.1.248;
CC -!- PATHWAY: One-carbon metabolism; methanogenesis from methylamine.
CC -!- SUBUNIT: Can form a complex with MtmC. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the monomethylamine methyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM31132.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM31133.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM33031.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM33032.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE008384; AAM31132.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE008384; AAM31133.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE008384; AAM33031.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE008384; AAM33032.1; ALT_SEQ; Genomic_DNA.
DR STRING; 192952.MM_1436; -.
DR EnsemblBacteria; AAM31132; AAM31132; MM_1436.
DR EnsemblBacteria; AAM31133; AAM31133; MM_1437.
DR EnsemblBacteria; AAM33031; AAM33031; MM_3335.
DR EnsemblBacteria; AAM33032; AAM33032; MM_3336.
DR KEGG; mma:MM_1436; -.
DR KEGG; mma:MM_1437; -.
DR KEGG; mma:MM_3335; -.
DR KEGG; mma:MM_3336; -.
DR PATRIC; fig|192952.21.peg.1662; -.
DR eggNOG; arCOG05143; Archaea.
DR HOGENOM; CLU_1154359_0_0_2; -.
DR UniPathway; UPA00643; -.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0043852; F:monomethylamine methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.460; -; 1.
DR InterPro; IPR008031; MtmB_MeTrfase.
DR InterPro; IPR036655; MtmB_sf.
DR Pfam; PF05369; MtmB; 1.
DR SUPFAM; SSF75098; SSF75098; 1.
PE 3: Inferred from homology;
KW Methanogenesis; Methyltransferase; Pyrrolysine; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..458
FT /note="Monomethylamine methyltransferase MtmB"
FT /id="PRO_0000216557"
FT NON_STD 202
FT /note="Pyrrolysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 458 AA; 50367 MW; 1017775FE433BAC7 CRC64;
MTFRKSFDCY DFYDRAKVGE KCTQDDWDLM KIPMKAMELK QKYGLDFKGE FVPTDKDMME
KLFQAGFEML LECGIYCTDT HRIVKYTEDE IWDAINNVQK EFTLGTGRDA VNVRKRSVGD
KRKPIVQGGP TGSPISEEVF MPVHMSYALE REVDTIVDGV MTSVRGKAPI PGSPYEVLAA
KTETRLIKQA CAMAGRPGMG IOGPETSLSA QGNISSDCMG GQISSDSHEV SQLNELKIDL
DAIAVIAHYK GNSDIIMDEQ MPIFGGYAGG IEETTIVDIA THINAFVMSS ASWHLDGPVH
IRWGSTNTRE TLTIAGWACA TISEFTDMLS GNQYYPCAGP CTEMCLLEAS AQSITDTASG
REILSGVASA KGVVTDKTTG MEARMMGEVA RATAGMEISE VNKVLNALVP LYEKNYATAP
AGKTFQECYD VKTITPTEEY MQVYDGARKK LEDLGLVF