ID MCRA_METFE Reviewed; 555 AA. AC P12971; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 13-SEP-2023, entry version 99. DE RecName: Full=Methyl-coenzyme M reductase subunit alpha; DE EC=2.8.4.1 {ECO:0000250|UniProtKB:P11558}; DE AltName: Full=Coenzyme-B sulfoethylthiotransferase alpha; GN Name=mcrA; OS Methanothermus fervidus. OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria; OC Methanobacteriales; Methanothermaceae; Methanothermus. OX NCBI_TaxID=2180; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3170483; DOI=10.1128/jb.170.10.4718-4726.1988; RA Weil C.F., Cram D.S., Sherf B.A., Reeve J.N.; RT "Structure and comparative analysis of the genes encoding component C of RT methyl coenzyme M reductase in the extremely thermophilic archaebacterium RT Methanothermus fervidus."; RL J. Bacteriol. 170:4718-4726(1988). CC -!- FUNCTION: Component of the methyl-coenzyme M reductase (MCR) I that CC catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2- CC (methylthio)ethanesulfonate) using coenzyme B (CoB or 7- CC mercaptoheptanoylthreonine phosphate) as reductant which results in the CC production of methane and the mixed heterodisulfide of CoB and CoM CC (CoM-S-S-CoB). This is the final step in methanogenesis. CC {ECO:0000250|UniProtKB:P11558}. CC -!- CATALYTIC ACTIVITY: CC Reaction=coenzyme B + methyl-coenzyme M = coenzyme M-coenzyme B CC heterodisulfide + methane; Xref=Rhea:RHEA:12532, ChEBI:CHEBI:16183, CC ChEBI:CHEBI:58286, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=2.8.4.1; CC Evidence={ECO:0000250|UniProtKB:P11558}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12533; CC Evidence={ECO:0000250|UniProtKB:P11558}; CC -!- COFACTOR: CC Name=coenzyme F430; Xref=ChEBI:CHEBI:60540; CC Evidence={ECO:0000250|UniProtKB:P11558}; CC Note=Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme CC F430 is a yellow nickel porphinoid. Methyl-coenzyme-M reductase is CC activated when the enzyme-bound coenzyme F430 is reduced to the Ni(I) CC oxidation state. {ECO:0000250|UniProtKB:P11558}; CC -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; methane CC from methyl-coenzyme M: step 1/1. {ECO:0000250|UniProtKB:P11558}. CC -!- SUBUNIT: MCR is a hexamer of two alpha, two beta, and two gamma chains, CC forming a dimer of heterotrimers. {ECO:0000250|UniProtKB:P11558}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11558}. CC -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase alpha subunit CC family. {ECO:0000305}. 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; J03375; AAA72197.1; -; Genomic_DNA. DR AlphaFoldDB; P12971; -. DR SMR; P12971; -. DR UniPathway; UPA00646; UER00699. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR Gene3D; 3.30.70.470; -; 1. DR Gene3D; 1.20.840.10; Methyl-coenzyme M reductase, alpha/beta subunit, C-terminal; 1. DR InterPro; IPR016212; Me_CoM_Rdtase_asu. DR InterPro; IPR008924; Me_CoM_Rdtase_asu/bsu_C. DR InterPro; IPR009047; Me_CoM_Rdtase_asu_C. DR InterPro; IPR003183; Me_CoM_Rdtase_asu_N. DR InterPro; IPR015811; Me_CoM_Rdtase_asu_N_sub1. DR InterPro; IPR015823; Me_CoM_Rdtase_asu_N_sub2. DR InterPro; IPR009024; Me_CoM_Rdtase_Fd-like_fold. DR NCBIfam; TIGR03256; met_CoM_red_alp; 1. DR Pfam; PF02249; MCR_alpha; 1. DR Pfam; PF02745; MCR_alpha_N; 1. DR PIRSF; PIRSF000262; MCR_alpha; 1. DR SUPFAM; SSF48081; Methyl-coenzyme M reductase alpha and beta chain C-terminal domain; 1. DR SUPFAM; SSF55088; Methyl-coenzyme M reductase subunits; 1. PE 3: Inferred from homology; KW Cytoplasm; Metal-binding; Methanogenesis; Methylation; Nickel; Transferase. FT CHAIN 1..555 FT /note="Methyl-coenzyme M reductase subunit alpha" FT /id="PRO_0000147450" FT BINDING 150 FT /ligand="coenzyme F430" FT /ligand_id="ChEBI:CHEBI:60540" FT /ligand_part="Ni" FT /ligand_part_id="ChEBI:CHEBI:28112" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P11558" FT BINDING 228 FT /ligand="coenzyme B" FT /ligand_id="ChEBI:CHEBI:58596" FT /ligand_note="ligand shared between two alpha subunits" FT /note="in chain A" FT /evidence="ECO:0000250|UniProtKB:P11558" FT BINDING 259..260 FT /ligand="coenzyme B" FT /ligand_id="ChEBI:CHEBI:58596" FT /ligand_note="ligand shared between two alpha subunits" FT /note="in chain A" FT /evidence="ECO:0000250|UniProtKB:P11558" FT BINDING 273 FT /ligand="coenzyme B" FT /ligand_id="ChEBI:CHEBI:58596" FT /ligand_note="ligand shared between two alpha subunits" FT /note="in chain B" FT /evidence="ECO:0000250|UniProtKB:P11558" FT BINDING 336 FT /ligand="coenzyme M" FT /ligand_id="ChEBI:CHEBI:58319" FT /evidence="ECO:0000250|UniProtKB:P11558" FT BINDING 448 FT /ligand="coenzyme M" FT /ligand_id="ChEBI:CHEBI:58319" FT /evidence="ECO:0000250|UniProtKB:P11558" SQ SEQUENCE 555 AA; 61550 MW; C2517AB56DA53D72 CRC64; MAEERKKLFV DALRKKFKEE PKERKTTFYT LGGWKQSERK KEFVEYGKKV AKERGIPAYN PDIGTPLGQR VLMPYQVSTT DTFVEGDDLH FVNNLAMQQF WDDIRRTVIV GLNHAHRILE RSLGKEVTPE TINHYLETVN HAMPGAAVVQ EHMVETHPGL TADSYVKVFT GNDELADEIE SCYLIDINKQ FPEHQAEQLK KAIGHTIWQA VRIPTIVSRT CDGATTSRWS AMQIGMSMIS AYKQAAGEAA TADFAYAAKH AEVIHLGTFL PVRRARGENE LGGVPFGFLA DIVQSSRVHY EDPVRVALDV VASGAMLYDQ IWLGSYMSGG VGFTQYATAS YTDNILDDFT YYGKEYVEDK YGGLAEAPHD FDTILDVATE VTLYSLDQYE EYPTLMEDHF GGSQRAAIAA AASGCSTAFA AGNAQAGLSG WYLSQILHKE CHARLGFYGY DLQDQCGAAN TYSIRSDEGL PAELRGPNYP NYAMNVGHLG EYAGIVQAAH IARGDADSLN PLVKVAFADD NLPFDWTNPR GEFAKGALRE FEPEGERDLI RPAGK //