ID MTMB1_METBA Reviewed; 458 AA. AC O30642; O52752; DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 6. DT 13-SEP-2023, entry version 101. DE RecName: Full=Monomethylamine methyltransferase MtmB1; DE Short=MMA methyltransferase 1; DE Short=MMAMT 1; DE EC=2.1.1.248; GN Name=mtmB1; Synonyms=mtmB; 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 FUNCTION. RC STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474, and NIH; RX PubMed=9642198; DOI=10.1128/jb.180.13.3432-3440.1998; RA Burke S.A., Lo S.L., Krzycki J.A.; RT "Clustered genes encoding the methyltransferases of methanogenesis from RT monomethylamine."; RL J. Bacteriol. 180:3432-3440(1998). RN [2] RP PROTEIN SEQUENCE OF 2-7; 22-28; 189-213; 251-255; 408-411 AND 453-458, AND RP MASS SPECTROMETRY. RC STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474; RX PubMed=11435424; DOI=10.1074/jbc.m102929200; RA James C.M., Ferguson T.K., Leykam J.F., Krzycki J.A.; RT "The amber codon in the gene encoding the monomethylamine methyltransferase RT isolated from Methanosarcina barkeri is translated as a sense codon."; RL J. Biol. Chem. 276:34252-34258(2001). RN [3] RP FUNCTION, AND CATALYTIC ACTIVITY. RC STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474; RX PubMed=9195968; DOI=10.1074/jbc.272.26.16570; RA Burke S.A., Krzycki J.A.; RT "Reconstitution of monomethylamine:coenzyme M methyl transfer with a RT corrinoid protein and two methyltransferases purified from Methanosarcina RT barkeri."; RL J. Biol. Chem. 272:16570-16577(1997). RN [4] RP PYRROLYSINE AT PYL-202. 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). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS), PYRROLYSINE AT PYL-202, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=12029132; DOI=10.1126/science.1069556; RA Hao B., Gong W., Ferguson T.K., James C.M., Krzycki J.A., Chan M.K.; RT "A new UAG-encoded residue in the structure of a methanogen RT methyltransferase."; RL Science 296:1462-1466(2002). CC -!- FUNCTION: Catalyzes the transfer of the methyl group from CC monomethylamine to the corrinoid cofactor of MtmC (MtmC1 or MtmC2). CC {ECO:0000269|PubMed:9195968, ECO:0000269|PubMed:9642198}. 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 Evidence={ECO:0000269|PubMed:9195968}; CC -!- PATHWAY: One-carbon metabolism; methanogenesis from methylamine. CC -!- SUBUNIT: Dimer of homotrimers. Can form a complex with MtmC (MtmC1 or CC MtmC2). CC -!- MASS SPECTROMETRY: Mass=50105; Mass_error=2; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:11435424}; CC -!- MISCELLANEOUS: MtmB1 transcript is abundant relative to the mtmB2 CC transcript. CC -!- SIMILARITY: Belongs to the monomethylamine methyltransferase family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life's jokers - Issue 25 of CC August 2002; CC URL="https://web.expasy.org/spotlight/back_issues/025"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF013713; AAC38636.3; -; Genomic_DNA. DR EMBL; AF046875; AAC38637.1; -; Genomic_DNA. DR PDB; 1L2Q; X-ray; 1.70 A; A=1-458. DR PDB; 1NTH; X-ray; 1.55 A; A=1-457. DR PDB; 1TV2; X-ray; 2.00 A; A=1-457. DR PDB; 1TV3; X-ray; 2.20 A; A=1-457. DR PDB; 1TV4; X-ray; 1.80 A; A=1-457. DR PDBsum; 1L2Q; -. DR PDBsum; 1NTH; -. DR PDBsum; 1TV2; -. DR PDBsum; 1TV3; -. DR PDBsum; 1TV4; -. DR SMR; O30642; -. DR BioCyc; MetaCyc:MONOMER-12210; -. DR BRENDA; 2.1.1.248; 3250. DR BRENDA; 2.1.1.249; 3250. DR UniPathway; UPA00643; -. DR EvolutionaryTrace; O30642; -. DR GO; GO:0043852; F:monomethylamine methyltransferase activity; IDA:MENGO. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.460; Monomethylamine methyltransferase MtmB; 1. DR InterPro; IPR008031; MtmB_MeTrfase. DR InterPro; IPR036655; MtmB_sf. DR Pfam; PF05369; MtmB; 1. DR SUPFAM; SSF75098; Monomethylamine methyltransferase MtmB; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Methanogenesis; Methyltransferase; KW Pyrrolysine; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:11435424" FT CHAIN 2..458 FT /note="Monomethylamine methyltransferase MtmB1" FT /id="PRO_0000216550" FT NON_STD 202 FT /note="Pyrrolysine" FT VARIANT 36 FT /note="A -> S (in strain: NIH)" FT VARIANT 219 FT /note="T -> A (in strain: NIH)" FT HELIX 9..18 FT /evidence="ECO:0007829|PDB:1NTH" FT STRAND 19..21 FT /evidence="ECO:0007829|PDB:1NTH" FT HELIX 24..28 FT /evidence="ECO:0007829|PDB:1NTH" FT HELIX 31..42 FT /evidence="ECO:0007829|PDB:1NTH" FT HELIX 56..73 FT /evidence="ECO:0007829|PDB:1NTH" FT STRAND 75..77 FT /evidence="ECO:0007829|PDB:1NTH" FT TURN 78..81 FT /evidence="ECO:0007829|PDB:1NTH" FT STRAND 82..84 FT /evidence="ECO:0007829|PDB:1NTH" FT HELIX 88..95 FT /evidence="ECO:0007829|PDB:1NTH" FT STRAND 101..105 FT /evidence="ECO:0007829|PDB:1NTH" FT HELIX 107..109 FT /evidence="ECO:0007829|PDB:1NTH" FT STRAND 111..114 FT /evidence="ECO:0007829|PDB:1NTH" FT STRAND 125..129 FT /evidence="ECO:0007829|PDB:1NTH" FT HELIX 137..139 FT /evidence="ECO:0007829|PDB:1NTH" FT HELIX 140..148 FT /evidence="ECO:0007829|PDB:1NTH" FT STRAND 155..157 FT /evidence="ECO:0007829|PDB:1TV4" FT STRAND 160..162 FT /evidence="ECO:0007829|PDB:1NTH" FT HELIX 174..193 FT /evidence="ECO:0007829|PDB:1NTH" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:1TV4" FT HELIX 210..214 FT /evidence="ECO:0007829|PDB:1NTH" FT STRAND 226..231 FT /evidence="ECO:0007829|PDB:1NTH" FT TURN 234..236 FT /evidence="ECO:0007829|PDB:1NTH" FT HELIX 240..251 FT /evidence="ECO:0007829|PDB:1NTH" FT STRAND 255..259 FT /evidence="ECO:0007829|PDB:1NTH" FT STRAND 266..268 FT /evidence="ECO:0007829|PDB:1NTH" FT HELIX 271..288 FT /evidence="ECO:0007829|PDB:1NTH" FT STRAND 292..296 FT /evidence="ECO:0007829|PDB:1NTH" FT TURN 301..303 FT /evidence="ECO:0007829|PDB:1NTH" FT HELIX 309..325 FT /evidence="ECO:0007829|PDB:1NTH" FT STRAND 330..333 FT /evidence="ECO:0007829|PDB:1NTH" FT STRAND 340..342 FT /evidence="ECO:0007829|PDB:1NTH" FT HELIX 343..359 FT /evidence="ECO:0007829|PDB:1NTH" FT STRAND 362..366 FT /evidence="ECO:0007829|PDB:1NTH" FT HELIX 370..372 FT /evidence="ECO:0007829|PDB:1NTH" FT HELIX 380..393 FT /evidence="ECO:0007829|PDB:1NTH" FT HELIX 398..410 FT /evidence="ECO:0007829|PDB:1NTH" FT TURN 411..414 FT /evidence="ECO:0007829|PDB:1NTH" FT HELIX 416..418 FT /evidence="ECO:0007829|PDB:1TV3" FT HELIX 425..428 FT /evidence="ECO:0007829|PDB:1NTH" FT TURN 431..434 FT /evidence="ECO:0007829|PDB:1NTH" FT HELIX 438..454 FT /evidence="ECO:0007829|PDB:1NTH" SQ SEQUENCE 458 AA; 50238 MW; CB75A20B1E5C0A2C CRC64; MTFRKSFDCY DFYDRAKVGE KCTQDDWDLM KIPMKAMELK QKYGLDFKGE FIPTDKDMME KLFKAGFEML LECGIYCTDT HRIVKYTEDE IWDAINNVQK EFVLGTGRDA VNVRKRSVGD KAKPIVQGGP TGSPISEDVF MPVHMSYALE KEVDTIVNGV MTSVRGKSPI PKSPYEVLAA KTETRLIKNA CAMAGRPGMG VOGPETSLSA QGNISADCTG GMTCTDSHEV SQLNELKIDL DAISVIAHYK GNSDIIMDEQ MPIFGGYAGG IEETTIVDVA THINAVLMSS ASWHLDGPVH IRWGSTNTRE TLMIAGWACA TISEFTDILS GNQYYPCAGP CTEMCLLEAS AQSITDTASG REILSGVASA KGVVTDKTTG MEARMMGEVA RATAGVEISE VNVILDKLVS LYEKNYASAP AGKTFQECYD VKTVTPTEEY MQVYDGARKK LEDLGLVF //