ID MTRA2_METRM Reviewed; 193 AA. AC D3E0P6; DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot. DT 23-MAR-2010, sequence version 1. DT 25-MAY-2022, entry version 54. DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit A 2 {ECO:0000255|HAMAP-Rule:MF_01093}; DE EC=2.1.1.86 {ECO:0000255|HAMAP-Rule:MF_01093}; DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit A 2 {ECO:0000255|HAMAP-Rule:MF_01093}; GN Name=mtrA2 {ECO:0000255|HAMAP-Rule:MF_01093}; OrderedLocusNames=mru_0441; OS Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 / OS OCM 146 / M1) (Methanobacterium ruminantium). OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria; OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter. OX NCBI_TaxID=634498; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1; RX PubMed=20126622; DOI=10.1371/journal.pone.0008926; RA Leahy S.C., Kelly W.J., Altermann E., Ronimus R.S., Yeoman C.J., RA Pacheco D.M., Li D., Kong Z., McTavish S., Sang C., Lambie S.C., RA Janssen P.H., Dey D., Attwood G.T.; RT "The genome sequence of the rumen methanogen Methanobrevibacter ruminantium RT reveals new possibilities for controlling ruminant methane emissions."; RL PLoS ONE 5:E8926-E8926(2010). CC -!- FUNCTION: Part of a complex that catalyzes the formation of methyl- CC coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- CC tetrahydromethanopterin. This is an energy-conserving, sodium-ion CC translocating step. {ECO:0000255|HAMAP-Rule:MF_01093}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + 2 CC Na(+)(in) = 5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M + 2 CC Na(+)(out); Xref=Rhea:RHEA:53492, ChEBI:CHEBI:29101, CC ChEBI:CHEBI:58103, ChEBI:CHEBI:58116, ChEBI:CHEBI:58286, CC ChEBI:CHEBI:58319; EC=2.1.1.86; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01093}; CC -!- COFACTOR: CC Name=5-hydroxybenzimidazolylcob(I)amide; Xref=ChEBI:CHEBI:60494; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01093}; CC Note=Binds 1 5-hydroxybenzimidazolylcobamide group. {ECO:0000255|HAMAP- CC Rule:MF_01093}; CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); methyl- CC coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: step CC 2/2. {ECO:0000255|HAMAP-Rule:MF_01093}. CC -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, MtrD, CC MtrE, MtrF, MtrG and MtrH. {ECO:0000255|HAMAP-Rule:MF_01093}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01093}; CC Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01093}. CC -!- SIMILARITY: Belongs to the MtrA family. {ECO:0000255|HAMAP- CC Rule:MF_01093}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001719; ADC46292.1; -; Genomic_DNA. DR RefSeq; WP_012955243.1; NC_013790.1. DR AlphaFoldDB; D3E0P6; -. DR SMR; D3E0P6; -. DR STRING; 634498.mru_0441; -. DR EnsemblBacteria; ADC46292; ADC46292; mru_0441. DR GeneID; 8770081; -. DR KEGG; mru:mru_0441; -. DR PATRIC; fig|634498.28.peg.443; -. DR eggNOG; arCOG03221; Archaea. DR HOGENOM; CLU_100863_1_0_2; -. DR OMA; ARMKIVS; -. DR OrthoDB; 89197at2157; -. DR UniPathway; UPA00640; UER00698. DR Proteomes; UP000008680; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro. DR GO; GO:0030269; F:tetrahydromethanopterin S-methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro. DR HAMAP; MF_01093; MtrA; 1. DR InterPro; IPR030688; MeTrfase_MtrA/MtxA. DR InterPro; IPR005778; MtrA. DR Pfam; PF04208; MtrA; 1. DR PIRSF; PIRSF500207; MtrA; 1. DR PIRSF; PIRSF009452; MtrA_MtxA; 1. DR TIGRFAMs; TIGR01111; mtrA; 1. PE 3: Inferred from homology; KW Cell membrane; Cobalt; Membrane; Methanogenesis; Methyltransferase; KW One-carbon metabolism; Reference proteome; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..193 FT /note="Tetrahydromethanopterin S-methyltransferase subunit FT A 2" FT /id="PRO_0000403060" FT TOPO_DOM 1..38 FT /note="Cytoplasmic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01093" FT TRANSMEM 39..58 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01093" FT TOPO_DOM 59..193 FT /note="Extracellular" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01093" FT REGION 174..193 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 84 FT /note="5'-hydroxybenzimidazolyl-cobamide cofactor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01093" SQ SEQUENCE 193 AA; 20713 MW; D126A067DFD95C74 CRC64; MADKKPTAEN WPVVSGDYIV GDPESPVAVT TLASHNEDIP AAAGAAIAGP CKTENLGIEK VVANIISNPN IRFLILCGAE VQGHITGQSF KALYENGCDP EKKKITGATG AIPFVENIPM EGVERFQQQL ELVDMIDNED GGAITAKVKE CIEKDPGAFE EDSLVIKIDE ERYSKKSSFV ESSSESEKIE SEA //