MTBA_METBA
ID MTBA_METBA Reviewed; 339 AA.
AC O30640; Q48928;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Methylcobamide:CoM methyltransferase MtbA;
DE EC=2.1.1.247 {ECO:0000269|PubMed:8702528};
DE AltName: Full=MT2-A;
DE AltName: Full=Methylcobamide:CoM methyltransferase II isozyme A;
DE AltName: Full=[Methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M;
GN Name=mtbA {ECO:0000303|PubMed:9642198};
GN Synonyms=cmtA {ECO:0000303|PubMed:8702528};
OS Methanosarcina barkeri.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=2208;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=NIH;
RX PubMed=8702528; DOI=10.1074/jbc.271.31.18725;
RA Leclerc G.M., Grahame D.A.;
RT "Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina
RT barkeri: physicochemical characterization, cloning, sequence analysis, and
RT heterologous gene expression.";
RL J. Biol. Chem. 271:18725-18731(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
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 [3]
RP PROTEIN SEQUENCE OF 2-25, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX PubMed=7635826; DOI=10.1128/jb.177.15.4410-4416.1995;
RA Burke S.A., Krzycki J.A.;
RT "Involvement of the 'A' isozyme of methyltransferase II and the 29-
RT kilodalton corrinoid protein in methanogenesis from monomethylamine.";
RL J. Bacteriol. 177:4410-4416(1995).
RN [4]
RP CHARACTERIZATION.
RX PubMed=8617801; DOI=10.1074/jbc.271.9.5189;
RA Ferguson D.J. Jr., Krzycki J.A., Grahame D.A.;
RT "Specific roles of methylcobamide:coenzyme M methyltransferase isozymes in
RT metabolism of methanol and methylamines in Methanosarcina barkeri.";
RL J. Biol. Chem. 271:5189-5194(1996).
RN [5]
RP CHARACTERIZATION.
RC STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX PubMed=9006042; DOI=10.1128/jb.179.3.846-852.1997;
RA Ferguson D.J. Jr., Krzycki J.A.;
RT "Reconstitution of trimethylamine-dependent coenzyme M methylation with the
RT trimethylamine corrinoid protein and the isozymes of methyltransferase II
RT from Methanosarcina barkeri.";
RL J. Bacteriol. 179:846-852(1997).
RN [6]
RP FUNCTION, AND SUBUNIT.
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 [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX PubMed=10852929; DOI=10.1074/jbc.m910218199;
RA Ferguson D.J. Jr., Gorlatova N., Grahame D.A., Krzycki J.A.;
RT "Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete
RT corrinoid protein and two methyltransferases purified from Methanosarcina
RT barkeri.";
RL J. Biol. Chem. 275:29053-29060(2000).
CC -!- FUNCTION: Methyltransferase involved in methanogenesis from
CC methylamines methanol pathway. Catalyzes the transfer of the methyl
CC group from the methylated corrinoid protein MtmC (MtmC1 or MtmC2) or
CC MtbC to coenzyme M, forming the substrate for coenzyme-B
CC sulfoethylthiotransferase. {ECO:0000269|PubMed:10852929,
CC ECO:0000269|PubMed:7635826, ECO:0000269|PubMed:8702528,
CC ECO:0000269|PubMed:9195968}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coenzyme M + methyl-Co(III)-[methylamine-specific corrinoid
CC protein] = Co(I)-[methylamine-specific corrinoid protein] + H(+) +
CC methyl-coenzyme M; Xref=Rhea:RHEA:18773, Rhea:RHEA-COMP:11120,
CC Rhea:RHEA-COMP:11121, ChEBI:CHEBI:15378, ChEBI:CHEBI:58286,
CC ChEBI:CHEBI:58319, ChEBI:CHEBI:85033, ChEBI:CHEBI:85035;
CC EC=2.1.1.247; Evidence={ECO:0000269|PubMed:10852929,
CC ECO:0000269|PubMed:7635826, ECO:0000269|PubMed:8702528,
CC ECO:0000269|PubMed:9195968};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC -!- ACTIVITY REGULATION: Inhibited by EDTA and EGTA.
CC -!- PATHWAY: One-carbon metabolism; methanogenesis from methylated amine.
CC -!- SUBUNIT: Copurifies with MtbC. {ECO:0000269|PubMed:9195968}.
CC -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC MtbA/MtaA subfamily. {ECO:0000305}.
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DR EMBL; U38919; AAC44214.1; -; Genomic_DNA.
DR EMBL; AF013713; AAC38632.1; -; Genomic_DNA.
DR AlphaFoldDB; O30640; -.
DR SMR; O30640; -.
DR BioCyc; MetaCyc:MON-12205; -.
DR BRENDA; 2.1.1.246; 3250.
DR BRENDA; 2.1.1.247; 3250.
DR SABIO-RK; O30640; -.
DR UniPathway; UPA00650; -.
DR GO; GO:0043833; F:[methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0043791; F:dimethylamine methyltransferase activity; IDA:MENGO.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:InterPro.
DR GO; GO:2001129; P:methane biosynthetic process from dimethylamine; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:InterPro.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:InterPro.
DR CDD; cd03307; Mta_CmuA_like; 1.
DR Gene3D; 3.20.20.210; -; 1.
DR InterPro; IPR006360; Mtase_MtaA_CmuA.
DR InterPro; IPR038071; UROD/MetE-like_sf.
DR InterPro; IPR000257; Uroporphyrinogen_deCOase.
DR Pfam; PF01208; URO-D; 1.
DR SUPFAM; SSF51726; SSF51726; 1.
DR TIGRFAMs; TIGR01463; mtaA_cmuA; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Metal-binding; Methanogenesis;
KW Methyltransferase; Transferase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7635826"
FT CHAIN 2..339
FT /note="Methylcobamide:CoM methyltransferase MtbA"
FT /id="PRO_0000187667"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT VARIANT 226
FT /note="V -> A (in strain: NIH)"
FT VARIANT 249
FT /note="G -> E (in strain: NIH)"
SQ SEQUENCE 339 AA; 36664 MW; 63708390ED84FB12 CRC64;
MAEYTPKERL YRALRKQQVD RMPAVCFTQT ATVEQMEACG AYWPEAHSDA EKMATLAEAA
HTVVGFEAVR VPFDITAEAE FFGCGIKAGD LKQQPSVIKP SVKNLEDLEK LKNYNLKEGR
IAVVLEAVKI LSEKYGKELP IIGSMIGPFS LAQHINGDAW FGNLFTGEEV VPALLDFCSD
FNVAYAKAMV ENGADTIAII DPTASYELIG GEFYEKYALP YQKKIVDAMK ELDVATVLHI
CGNTTNGLGI MDKTGVNGIS VDQKVDIKTA TGSVKNAIIV GNLDPVAVLW NGTPEEIAEA
SKKALDAGVG LLTVGCGTVS MTPTVNLQKM IECAKSHTY
