MCRA_METVO
ID MCRA_METVO Reviewed; 555 AA.
AC P11559;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 98.
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 Methanococcus voltae.
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=2188;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS;
RX PubMed=3185509; DOI=10.1007/bf00339610;
RA Klein A., Allmansberger R., Bokranz M., Knaub S., Mueller B., Muth E.;
RT "Comparative analysis of genes encoding methyl coenzyme M reductase in
RT methanogenic bacteria.";
RL Mol. Gen. Genet. 213:409-420(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; X07793; CAA30633.1; -; Genomic_DNA.
DR PIR; S03261; S03261.
DR AlphaFoldDB; P11559; -.
DR SMR; P11559; -.
DR PRIDE; P11559; -.
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_0000147461"
FT BINDING 152
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 230
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 261..262
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 275
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 337
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; 61227 MW; DCBCE5DC91EA69D5 CRC64;
MEAEKRLFLK ALKEKFEEDP KEKFTKFYTY GGWQQSARKQ EFVSENEKIV AEKRGGIPMY
NPDIGVPLGQ RKLMPYKISN TDTYVEGDDL HFMNNAAIQQ LWDDIRRTVI VGMDTAHMVL
EKRLGVEVTP ETINEYMHTI NHSLPGGAAV VQEHMVEVHP SLAWDCYAKI FTGDDELADE
LDDRFVIDIN KLFPEEQAEA SKAAIGKKTY QVSRVPSLVG RVCDGGTISR WSAMQIGMSF
ITAYKLCAGE AAIADFSYAA KHADVIQMGN ALLGRRARGP NELGGVRFGI LSDVVQTTRV
SDDPVEQSLE VVATGAALYD QIWLGSYMSG GVGFTQYATA SYTDDILDDF SYYGYEYVEK
KYGRCGTKAT MDVVEDIASE VTLYALEQYD EYPALLEDHF GGSQRAAVAA AAAGISVCMA
TGNSNAGVNG WYLSQILHKE YHSRLGFYGY DLQDQCGASN SLAIRNDEAS PLELRGPNYP
NYAMNVGHQG EYAGIAQSAH SARGDAFATN ALIKVAFADP SLVFDFSKPR KEIARGALRE
FEAAGERDPI LPAKI
