ID MTSA_METMA Reviewed; 367 AA.
AC Q8PUA8;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 114.
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; OrderedLocusNames=MM_2427;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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 (By
CC similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; AE008384; AAM32123.1; -; Genomic_DNA.
DR RefSeq; WP_011034351.1; NC_003901.1.
DR AlphaFoldDB; Q8PUA8; -.
DR SMR; Q8PUA8; -.
DR GeneID; 82161505; -.
DR KEGG; mma:MM_2427; -.
DR PATRIC; fig|192952.21.peg.2778; -.
DR eggNOG; arCOG03325; Archaea.
DR HOGENOM; CLU_040933_2_1_2; -.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044683; F:methylthiol:coenzyme M methyltransferase activity; IEA:UniProtKB-EC.
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 NCBIfam; TIGR01463; mtaA_cmuA; 1.
DR PANTHER; PTHR47099; METHYLCOBAMIDE:COM METHYLTRANSFERASE MTBA; 1.
DR PANTHER; PTHR47099:SF1; METHYLCOBAMIDE:COM METHYLTRANSFERASE MTBA; 1.
DR Pfam; PF01208; URO-D; 1.
DR SUPFAM; SSF51726; UROD/MetE-like; 1.
PE 3: Inferred from homology;
KW Metal-binding; Methanogenesis; Methyltransferase; Transferase; Zinc.
FT CHAIN 1..367
FT /note="Methylated-thiol--coenzyme M methyltransferase"
FT /id="PRO_0000419107"
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; 40192 MW; 1036FC6F5D158A2B CRC64;
MVSEMTPTRR ALAAVLGGRV DYVPPANPLA QTTTELMAIC NASWPKAHFD SKMMADLAAA
SYEVCGIEAA RPQFDISLEA EVLGCKLDWD KPDRPPVTGP AYTNPEDVTW PDKLEETGRI
PVVLGAIDEL RKRYDGMLPI IPLLTAPFTV AGHIAGVENM ARWTKTDPEK AHAFIDAATD
FVVAYGKLQA AYGAHILFLA DPSASSSLIS AETYREFVLP AHRRLAKEIS CPQILHICGD
SSKLLPYIKQ SGIDCFSFDT VPVWYCRQVI GNDMSILGSL DVIDLMPNGT PEQVYNRTRE
CILQGTDIVG TACGVSYGTP LENLRAYVRA CKETPIPRYD DVEDLIRQIG VGIGRNMKEN
VLGGMQE
//
