MTAA_METBF
ID MTAA_METBF Reviewed; 339 AA.
AC Q48949; Q46DM0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Methylcobamide:CoM methyltransferase MtaA;
DE EC=2.1.1.246;
DE AltName: Full=Methylcobalamin: Coenzyme M methyltransferase;
DE AltName: Full=[Methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M methyltransferase;
GN Name=mtaA; OrderedLocusNames=Mbar_A1054;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21; 39-55 AND
RP 303-32, AND FUNCTION.
RC STRAIN=Fusaro / DSM 804;
RX PubMed=8654414; DOI=10.1111/j.1432-1033.1996.00653.x;
RA Harms U., Thauer R.K.;
RT "Methylcobalamin: coenzyme M methyltransferase isoenzymes MtaA and MtbA
RT from Methanosarcina barkeri. Cloning, sequencing and differential
RT transcription of the encoding genes, and functional overexpression of the
RT mtaA gene in Escherichia coli.";
RL Eur. J. Biochem. 235:653-659(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
RN [3]
RP IDENTIFICATION.
RC STRAIN=Fusaro / DSM 804;
RX PubMed=6438059; DOI=10.1128/jb.160.2.629-635.1984;
RA van der Meijden P., te Brommelstroet B.W., Poirot C.M., van der Drift C.,
RA Vogels G.D.;
RT "Purification and properties of methanol:5-hydroxybenzimidazolylcobamide
RT methyltransferase from Methanosarcina barkeri.";
RL J. Bacteriol. 160:629-635(1984).
RN [4]
RP FUNCTION.
RC STRAIN=Fusaro / DSM 804;
RX PubMed=10215883; DOI=10.1046/j.1432-1327.1999.00355.x;
RA Sauer K., Thauer R.K.;
RT "Methanol:coenzyme M methyltransferase from Methanosarcina barkeri
RT -- substitution of the corrinoid harbouring subunit MtaC by free
RT cob(I)alamin.";
RL Eur. J. Biochem. 261:674-681(1999).
RN [5]
RP COFACTOR, AND ZINC-BINDING.
RC STRAIN=Fusaro / DSM 804;
RX PubMed=10785368; DOI=10.1046/j.1432-1327.2000.01245.x;
RA Sauer K., Thauer R.K.;
RT "Methyl-coenzyme M formation in methanogenic archaea. Involvement of zinc
RT in coenzyme M activation.";
RL Eur. J. Biochem. 267:2498-2504(2000).
RN [6]
RP COFACTOR, ZINC-BINDING, AND MUTAGENESIS OF HIS-237 AND CYS-239.
RC STRAIN=Fusaro / DSM 804;
RX PubMed=11985589; DOI=10.1046/j.1432-1033.2002.02860.x;
RA Kruer M., Haumann M., Meyer-Klaucke W., Thauer R.K., Dau H.;
RT "The role of zinc in the methylation of the coenzyme M thiol group in
RT methanol:coenzyme M methyltransferase from Methanosarcina barkeri.";
RL Eur. J. Biochem. 269:2117-2123(2002).
CC -!- FUNCTION: Methyltransferase involved in methanogenesis in the methanol
CC pathway. Catalyzes the transfer of the methyl group from the methylated
CC corrinoid protein MtaC to coenzyme M, forming the substrate for
CC coenzyme-B sulfoethylthiotransferase. MtaC can be substituted by free
CC cob(I)alamin in vitro. {ECO:0000269|PubMed:10215883,
CC ECO:0000269|PubMed:8654414}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coenzyme M + methyl-Co(III)-[methanol-specific corrinoid
CC protein] = Co(I)-[methanol-specific corrinoid protein] + H(+) +
CC methyl-coenzyme M; Xref=Rhea:RHEA:45208, Rhea:RHEA-COMP:17570,
CC Rhea:RHEA-COMP:17571, ChEBI:CHEBI:15378, ChEBI:CHEBI:16379,
CC ChEBI:CHEBI:58286, ChEBI:CHEBI:58319, ChEBI:CHEBI:60494;
CC EC=2.1.1.246;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:10785368, ECO:0000269|PubMed:11985589};
CC Note=Zn(2+) is involved in coenzyme M activation: in the absence of
CC coenzyme M, zinc is coordinated by a single sulfur ligand and three
CC oxygen or nitrogen ligands. In the presence of coenzyme M, one
CC oxygen/nitrogen-ligand is replaced by sulfur, probably due to ligation
CC of the thiol group of coenzyme M. {ECO:0000269|PubMed:10785368,
CC ECO:0000269|PubMed:11985589};
CC -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC MtbA/mtaA subfamily. {ECO:0000305}.
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DR EMBL; X91893; CAA62995.1; -; Genomic_DNA.
DR EMBL; CP000099; AAZ70022.1; -; Genomic_DNA.
DR PIR; S62368; S62368.
DR AlphaFoldDB; Q48949; -.
DR SMR; Q48949; -.
DR STRING; 269797.Mbar_A1054; -.
DR EnsemblBacteria; AAZ70022; AAZ70022; Mbar_A1054.
DR KEGG; mba:Mbar_A1054; -.
DR eggNOG; arCOG03324; Archaea.
DR HOGENOM; CLU_040933_2_1_2; -.
DR OMA; YERYCAP; -.
DR BioCyc; MetaCyc:MTAAMBARK-MON; -.
DR BRENDA; 2.1.1.246; 3250.
DR BRENDA; 2.1.1.90; 3250.
DR GO; GO:1990088; F:[methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M methyltransferase; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:InterPro.
DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
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 CHAIN 1..339
FT /note="Methylcobamide:CoM methyltransferase MtaA"
FT /id="PRO_0000418939"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT MUTAGEN 237
FT /note="H->A: Strongly impaired methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:11985589"
FT MUTAGEN 239
FT /note="C->A: Strongly impaired methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:11985589"
SQ SEQUENCE 339 AA; 35872 MW; 7721263F2F9561EB CRC64;
MSEFTLKTRL LAALEGKPVD KVPVCSVTQT GIVELMDKVG AAWPEAHTNP ELMAKLAIAN
YELSGLEAVR LPYCLTVLGE AMGCEINMGT KNRQPSVTAS PYPKNLDGAV VPADLLQRNR
IPAVLEAIKI VREKVGPDVP IIGGMEGPVT LASDLISVKS FMKWSIKKTD LFEQALDISA
EAAIAYANAM VEAGADVIAI ADPVASPDLM SPETFKQFLQ SRLQKFSAGV NSVTVLHICG
KVNAILSDMA DCGFEGLSVE EKIGTAAEGK KIIGDRARLV GNISSPFTLL PGPIDKIKAE
AKVALEGGID VLAPGCGIAP MTPLENVKAL VAARDEYYA
