MCRA_METFE
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 03-AUG-2022, entry version 96.
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}.
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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; 1.20.840.10; -; 1.
DR Gene3D; 3.30.70.470; -; 1.
DR Gene3D; 3.90.390.10; -; 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 Pfam; PF02249; MCR_alpha; 1.
DR Pfam; PF02745; MCR_alpha_N; 1.
DR PIRSF; PIRSF000262; MCR_alpha; 1.
DR SUPFAM; SSF48081; SSF48081; 1.
DR SUPFAM; SSF55088; SSF55088; 1.
DR TIGRFAMs; TIGR03256; met_CoM_red_alp; 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
