ID   MTSA_METBA              Reviewed;         367 AA.
AC   Q48924;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Methylated-thiol--coenzyme M methyltransferase;
DE            EC=2.1.1.251;
DE   AltName: Full=Methylthiol:coenzyme M methyltransferase 40 kDa subunit;
GN   Name=mtsA;
OS   Methanosarcina barkeri.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2208;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX   PubMed=8932317; DOI=10.1128/jb.178.22.6599-6607.1996;
RA   Paul L., Krzycki J.A.;
RT   "Sequence and transcript analysis of a novel Methanosarcina barkeri
RT   methyltransferase II homolog and its associated corrinoid protein
RT   homologous to methionine synthase.";
RL   J. Bacteriol. 178:6599-6607(1996).
RN   [2]
RP   FUNCTION.
RC   STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX   PubMed=9371433; DOI=10.1128/jb.179.22.6902-6911.1997;
RA   Tallant T.C., Krzycki J.A.;
RT   "Methylthiol:coenzyme M methyltransferase from Methanosarcina barkeri, an
RT   enzyme of methanogenesis from dimethylsulfide and
RT   methylmercaptopropionate.";
RL   J. Bacteriol. 179:6902-6911(1997).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX   PubMed=11073950; DOI=10.1074/jbc.m007514200;
RA   Tallant T.C., Paul L., Krzycki J.A.;
RT   "The MtsA subunit of the methylthiol:coenzyme M methyltransferase of
RT   Methanosarcina barkeri catalyses both half-reactions of corrinoid-dependent
RT   dimethylsulfide: coenzyme M methyl transfer.";
RL   J. Biol. Chem. 276:4485-4493(2001).
CC   -!- FUNCTION: Methyltransferase involved in methanogenesis from methylated-
CC       thiols. Catalyzes two successive steps: mediates the transfer of a
CC       methyl group from the substrate to the cobalt cofactor of a methylated-
CC       thiol-specific corrinoid protein (MtsB), and the subsequent transfer of
CC       the methyl group from the corrinoid protein to coenzyme M.
CC       {ECO:0000269|PubMed:11073950, ECO:0000269|PubMed:9371433}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=coenzyme M + methanethiol = H(+) + hydrogen sulfide + methyl-
CC         coenzyme M; Xref=Rhea:RHEA:32667, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16007, ChEBI:CHEBI:29919, ChEBI:CHEBI:58286,
CC         ChEBI:CHEBI:58319; EC=2.1.1.251;
CC         Evidence={ECO:0000269|PubMed:11073950};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:11073950};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:11073950};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5.5 mM for methyl-CoM {ECO:0000269|PubMed:11073950};
CC         KM=10.8 mM for coenzyme M {ECO:0000269|PubMed:11073950};
CC         Vmax=103 umol/min/mg enzyme with methyl-CoM as substrate
CC         {ECO:0000269|PubMed:11073950};
CC         Vmax=21 umol/min/mg enzyme with coenzyme M as substrate
CC         {ECO:0000269|PubMed:11073950};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; U36337; AAC46230.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q48924; -.
DR   SMR; Q48924; -.
DR   BioCyc; MetaCyc:MON-12241; -.
DR   BRENDA; 2.1.1.251; 3250.
DR   SABIO-RK; Q48924; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044683; F:methylthiol:coenzyme M methyltransferase activity; IDA:MENGO.
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   Metal-binding; Methanogenesis; Methyltransferase; Transferase; Zinc.
FT   CHAIN           1..367
FT                   /note="Methylated-thiol--coenzyme M methyltransferase"
FT                   /id="PRO_0000419106"
FT   BINDING         236
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   367 AA;  40205 MW;  0D39ABE447F453D6 CRC64;
     MVSEMTPTRR VMAAVLGGRV DYVPPANPLA QTTTELMQIC NASWPKAHFD SKMMADLAAA
     PYEICGIEAA RPQFDISLEA EVLGCKLDWN KPDRPPVTGP AYTDPADITW PDNLEEAGRI
     PVVLGAIEEL RKRYDGMLPV IPVLTSPFTV AGHIAGVENL VRWTKTDPEK AHAFIEAATD
     FVIAYGKLQT AYGAHILFPA DPSASGDLIS GETYKEFVLP AHKRMAKEIS CPLILHICGD
     TSKLLPYIKQ SGIDCFSFDA VPVWYCRQVM GNEMSILGSL DVIDLMPNGT PEQVYNRTRE
     CILQGADIVG TACDVSFGTS LENLRAYVRA CKETPIPKYD DVEDIIRQIG VGIGRNMKEN
     VLGGMQK