ID A0A166CWD2_9EURY Unreviewed; 551 AA.
AC A0A166CWD2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Methyl-coenzyme M reductase subunit alpha {ECO:0000256|PIRNR:PIRNR000262};
DE EC=2.8.4.1 {ECO:0000256|PIRNR:PIRNR000262};
GN ORFNames=MBCUT_02940 {ECO:0000313|EMBL:KZX17247.1};
OS Methanobrevibacter cuticularis.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=47311 {ECO:0000313|EMBL:KZX17247.1, ECO:0000313|Proteomes:UP000077275};
RN [1] {ECO:0000313|EMBL:KZX17247.1, ECO:0000313|Proteomes:UP000077275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11139 {ECO:0000313|EMBL:KZX17247.1,
RC ECO:0000313|Proteomes:UP000077275};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanobrevibacter cuticularis DSM 11139.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|PIRNR:PIRNR000262}.
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:0000256|ARBA:ARBA00000951};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12533;
CC Evidence={ECO:0000256|ARBA:ARBA00000951};
CC -!- COFACTOR:
CC Name=coenzyme F430; Xref=ChEBI:CHEBI:60540;
CC Evidence={ECO:0000256|PIRNR:PIRNR000262};
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:0000256|PIRNR:PIRNR000262};
CC -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; methane
CC from methyl-coenzyme M: step 1/1. {ECO:0000256|ARBA:ARBA00005149,
CC ECO:0000256|PIRNR:PIRNR000262}.
CC -!- SUBUNIT: Hexamer of two alpha, two beta, and two gamma chains.
CC {ECO:0000256|PIRNR:PIRNR000262}.
CC -!- SUBUNIT: MCR is a hexamer of two alpha, two beta, and two gamma chains,
CC forming a dimer of heterotrimers. {ECO:0000256|ARBA:ARBA00011155}.
CC -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase alpha subunit
CC family. {ECO:0000256|ARBA:ARBA00010434}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZX17247.1}.
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DR EMBL; LWMW01000054; KZX17247.1; -; Genomic_DNA.
DR RefSeq; WP_067257927.1; NZ_LWMW01000054.1.
DR AlphaFoldDB; A0A166CWD2; -.
DR STRING; 47311.MBCUT_02940; -.
DR PATRIC; fig|47311.3.peg.324; -.
DR OrthoDB; 52468at2157; -.
DR UniPathway; UPA00646; UER00699.
DR Proteomes; UP000077275; Unassembled WGS sequence.
DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-UniRule.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000262};
KW Methanogenesis {ECO:0000256|ARBA:ARBA00022994,
KW ECO:0000256|PIRNR:PIRNR000262};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|PIRNR:PIRNR000262};
KW Reference proteome {ECO:0000313|Proteomes:UP000077275};
KW Transferase {ECO:0000256|PIRNR:PIRNR000262}.
FT DOMAIN 4..268
FT /note="Methyl-coenzyme M reductase alpha subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02745"
FT DOMAIN 316..442
FT /note="Methyl-coenzyme M reductase alpha subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02249"
FT BINDING 147
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:0000256|PIRSR:PIRSR000262-1"
FT MOD_RES 257
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000262-2"
FT MOD_RES 271
FT /note="5-methylarginine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000262-2"
SQ SEQUENCE 551 AA; 60678 MW; A34E0EFC156AFE24 CRC64;
MANKKFIEAL NKKFKESPEE KTTTFYNLGG WKQSERKSEF AKEGKEIATK RGIPQYNPDV
GSPLGQRALM PYQVSTTETF VEGDDFHFVN NAAIQQMWDD IRRTVIVGLN TAHTVLEKRL
GIEVTPETIT EYLETVNHAM PGAAVVQEHM VETNPALVAD SYVKIFTGDD EVADEIDSAF
VLDINKEFSK EQAEALKAEV GDKIWQVVRI PSIVGRVCDG GTTSRWSAMQ IGMSMISAYN
QCAGEGATGD FAYASKHAEV IHMGTYLPVR RARAENEPGG IPFGYMADIC QSSRVNEDDP
VRTTLDVVAM SAALYDQIWL GSYMSGGVGF TQYASAAYTD NVLDDFTYYG KEYVEDKYGG
LCEAPNNMDT VLDVGSEVTF YGLEQYEEYP ALLETQFGGS QRASVVSAAA GCSTAFATGN
AQTGLSAWYL SMYLHKEQHS RLGFYGYDLQ DQCGASNVFS IRADEGLPVE MRGPNYPNYA
MNVGHQGEYA GISQAPHAAR KDAFAFNPLI KIAFADKNLS FDFSQPRAEI AKGALREFMP
DGERSLIIPA K
//
