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 16-JUN-2009, entry version 65. DE RecName: Full=Monomethylamine methyltransferase mtmB1; DE Short=MMA methyltransferase 1; DE Short=MMAMT 1; DE EC=2.1.1.-; GN Name=mtmB1; Synonyms=mtmB; OS Methanosarcina barkeri. OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=2208; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474, and NIH; RX MEDLINE=98317284; PubMed=9642198; RA Burke S.A., Lo S.L., Krzycki J.A.; RT "Clustered genes encoding the methyltransferases of methanogenesis RT from 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, RP AND MASS SPECTROMETRY. RC STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474; RX MEDLINE=21423961; 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 RT methyltransferase isolated from Methanosarcina barkeri is translated RT as a sense codon."; RL J. Biol. Chem. 276:34252-34258(2001). RN [3] RP CHARACTERIZATION. RC STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474; RX MEDLINE=97341199; 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 RT Methanosarcina 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., RA Wolff J.J., 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), MASS SPECTROMETRY, AND RP PYRROLYSINE AT PYL-202. RX MEDLINE=22025705; 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. CC -!- PATHWAY: One-carbon metabolism; methanogenesis from methylamine. CC -!- SUBUNIT: Dimer of homotrimers. Can form a complex with mtmC. CC -!- MASS SPECTROMETRY: Mass=50105; Mass_error=2; Method=Electrospray; CC Range=2-458; Source=PubMed:11435424; CC -!- MISCELLANEOUS: MtmB1 transcript is abundant relative to the mtmB2 CC transcript. CC -!- SIMILARITY: Belongs to the monomethylamine methyltransferase CC family. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life's jokers - Issue CC 25 of August 2002; CC URL="http://www.expasy.org/spotlight/back_issues/sptlt025.shtml"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs 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=1-458. DR PDB; 1TV2; X-ray; 2.00 A; A=1-458. DR PDB; 1TV3; X-ray; 2.20 A; A=1-458. DR PDB; 1TV4; X-ray; 1.80 A; A=1-458. DR PDBsum; 1L2Q; -. DR PDBsum; 1NTH; -. DR PDBsum; 1TV2; -. DR PDBsum; 1TV3; -. DR PDBsum; 1TV4; -. DR BioCyc; MetaCyc:MON-12210; -. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR InterPro; IPR008031; MtmB_MeTrfase. DR Pfam; PF05369; MtmB; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Methanogenesis; KW Methyltransferase; Pyrrolysine; Transferase. FT INIT_MET 1 1 Removed. FT CHAIN 2 458 Monomethylamine methyltransferase mtmB1. FT /FTId=PRO_0000216550. FT NON_STD 202 202 Pyrrolysine. FT VARIANT 36 36 A -> S (in strain: NIH). FT VARIANT 219 219 T -> A (in strain: NIH). FT HELIX 9 18 FT STRAND 19 21 FT HELIX 24 28 FT HELIX 31 42 FT HELIX 56 73 FT STRAND 75 77 FT TURN 78 81 FT STRAND 82 84 FT HELIX 88 95 FT STRAND 101 105 FT HELIX 107 109 FT STRAND 111 114 FT STRAND 125 129 FT HELIX 137 139 FT HELIX 140 148 FT STRAND 155 157 FT STRAND 160 162 FT HELIX 174 193 FT STRAND 201 203 FT HELIX 210 214 FT STRAND 226 231 FT TURN 234 236 FT HELIX 240 251 FT STRAND 255 259 FT STRAND 266 268 FT HELIX 271 288 FT STRAND 292 296 FT TURN 301 303 FT HELIX 309 325 FT STRAND 330 333 FT STRAND 340 342 FT HELIX 343 359 FT STRAND 362 366 FT HELIX 370 372 FT HELIX 380 393 FT HELIX 398 410 FT TURN 411 414 FT HELIX 425 428 FT TURN 431 434 FT HELIX 438 453 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 //