ID A0A120K0D9_9EURY Unreviewed; 551 AA.
AC A0A120K0D9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=TL18_09320 {ECO:0000313|EMBL:AMD18197.1};
OS Methanobrevibacter sp. YE315.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=1609968 {ECO:0000313|EMBL:AMD18197.1, ECO:0000313|Proteomes:UP000057992};
RN [1] {ECO:0000313|EMBL:AMD18197.1, ECO:0000313|Proteomes:UP000057992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YE315 {ECO:0000313|EMBL:AMD18197.1,
RC ECO:0000313|Proteomes:UP000057992};
RA Ouwerkerk D., Gilbert R.A., Klieve A.V., Martinez E.;
RT "Genome sequence of Methanobrevibacter sp. YE315.";
RL Submitted (JAN-2015) 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 ---------------------------------------------------------------------------
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; CP010834; AMD18197.1; -; Genomic_DNA.
DR RefSeq; WP_067044659.1; NZ_CP010834.1.
DR AlphaFoldDB; A0A120K0D9; -.
DR SMR; A0A120K0D9; -.
DR STRING; 1609968.TL18_09320; -.
DR GeneID; 28488058; -.
DR KEGG; meye:TL18_09320; -.
DR PATRIC; fig|1609968.3.peg.1899; -.
DR OrthoDB; 52468at2157; -.
DR UniPathway; UPA00646; UER00699.
DR Proteomes; UP000057992; 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}.
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; 60344 MW; EB6D7E8064097A3D CRC64;
MADKKFLDAM KKKFVEDPTE KTTQFYNMGG WTQSERKTAF VNEGKEIAEK RGIPMYNPDI
GSPLGQRALM SYQLSTTDTF VEGDDLHYIN NAAIQQAWDD IRRTVIVGLN TAHNVLEKRL
GIEVTPETIT NYLETVNHAM PGAAVVQEHM VETDPLVVAD SYVKVFTGDD ELADEIDSAF
VLDINKEFPE DQAEALKAEV GGAIWQAVRI PSIVGRVCDG GNTSRWSAMQ IGMSMISAYN
QCAGEGATGD FAYASKHAEV VHMGTYLPVR RARAENELGG VPFGFMADIC QGSRAYPDDP
VRSTLEVVAL GAALYDQIWL GSYMSGGVGF TQYATAAYTD NVLDDFTYYG KDYVEDKYGD
LCSAPNNMDT VLDVGSEVAF YALEQYESYP ALLETHFGGS QRASVISAAA GCSTAFATGN
AQTGLSAWYL SMYLHKEQHS RLGFYGFDLQ DQCGAANVFS IRNDEGLPLE MRGPNYPNYA
MNVGHQGEYA GISQAPHSAR GDAWAFNPLV KIAFADKNLC FDFSQVRAQF AKGALREFEP
AGERTAITPA K
//
