ID F6D2D3_METPW Unreviewed; 551 AA.
AC F6D2D3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Methyl-coenzyme M reductase subunit alpha {ECO:0000256|PIRNR:PIRNR000262};
DE EC=2.8.4.1 {ECO:0000256|PIRNR:PIRNR000262};
GN OrderedLocusNames=MSWAN_2056 {ECO:0000313|EMBL:AEG19065.1};
OS Methanobacterium paludis (strain DSM 25820 / JCM 18151 / SWAN1).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=868131 {ECO:0000313|EMBL:AEG19065.1, ECO:0000313|Proteomes:UP000009231};
RN [1] {ECO:0000313|Proteomes:UP000009231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25820 / JCM 18151 / SWAN1
RC {ECO:0000313|Proteomes:UP000009231};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Chertkov O., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Cadillo-Quiroz H.,
RA Imachi H., Zinder S., Liu W., Woyke T.;
RT "Complete sequence of Methanobacterium sp. SWAN-1.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEG19065.1, ECO:0000313|Proteomes:UP000009231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25820 / JCM 18151 / SWAN1
RC {ECO:0000313|Proteomes:UP000009231};
RX PubMed=24449792; DOI=10.1099/ijs.0.059964-0;
RA Cadillo-Quiroz H., Brauer S.L., Goodson N., Yavitt J.B., Zinder S.H.;
RT "Methanobacterium paludis sp. nov. and a novel strain of Methanobacterium
RT lacus isolated from northern peatlands.";
RL Int. J. Syst. Evol. Microbiol. 64:1473-1480(2014).
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}.
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DR EMBL; CP002772; AEG19065.1; -; Genomic_DNA.
DR RefSeq; WP_013826564.1; NC_015574.1.
DR AlphaFoldDB; F6D2D3; -.
DR STRING; 868131.MSWAN_2056; -.
DR GeneID; 10669574; -.
DR KEGG; mew:MSWAN_2056; -.
DR eggNOG; arCOG04857; Archaea.
DR HOGENOM; CLU_493170_0_0_2; -.
DR OrthoDB; 52468at2157; -.
DR UniPathway; UPA00646; UER00699.
DR Proteomes; UP000009231; Chromosome.
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 Transferase {ECO:0000256|PIRNR:PIRNR000262, ECO:0000313|EMBL:AEG19065.1}.
FT DOMAIN 3..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; 60491 MW; 92237AA7A518E6B4 CRC64;
MADKKFIDAL NKKFKEDPEE KKTTFYSFGG WKQSERKREF VEAGKKIAAE RGIPQYNPDV
GTPLGQRVLM PYQVSTTDTF VEGDDLHFVN NAAMQQMWDD IRRTVIVGLD TAHNVIEKRL
GKEVTPETIT HYLETVNHAM PGAAVVQEHM VETNPALVAD SYVKVFTGND EIADEIDSAY
VLDINKMFPE EQAEVLKAEV GDGIWQAVRI PTIVSRTCDG GTTSRWSAMQ IGMSMISAYK
QCAGEAATGD FAFAAKHAAV IHMGTALPQR RARGENEPGG IPFGYLADIC QSSRKYADDP
VRVTLDVVAT GAMLYDQIWL GSYMSGGVGF TQYATAAYTD NVLDDFCYYG KEYVEDKFGG
LCEAPNTMET VLDVGSEVTF YALEQYEEYP ALLETQFGGS QRAAVTAAAA GCSTGFATGN
AQTGLSAWYL SMYLHKEQHS RLGFYGYDLQ DQCGAANVFA IRGDEGLPTE LRGPNYPNYA
MNVGHQGEYA GIAQSAHAAR KDAFVLNPLV KIAFADDNLA FDFSEVRAEF AKGALREFEP
AGERDLITPA K
//
