MTMB1_METBA
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 03-AUG-2022, entry version 98.
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";
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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:MON-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; -; 1.
DR InterPro; IPR008031; MtmB_MeTrfase.
DR InterPro; IPR036655; MtmB_sf.
DR Pfam; PF05369; MtmB; 1.
DR SUPFAM; SSF75098; SSF75098; 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
