ID A0A0E3SA85_9EURY Unreviewed; 570 AA.
AC A0A0E3SA85;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=MSHOH_0084 {ECO:0000313|EMBL:AKB76567.1};
OS Methanosarcina horonobensis HB-1 = JCM 15518.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=1434110 {ECO:0000313|EMBL:AKB76567.1, ECO:0000313|Proteomes:UP000033101};
RN [1] {ECO:0000313|EMBL:AKB76567.1, ECO:0000313|Proteomes:UP000033101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HB-1 {ECO:0000313|EMBL:AKB76567.1,
RC ECO:0000313|Proteomes:UP000033101};
RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT "Methanogenic archaea and the global carbon cycle.";
RL Submitted (JUL-2014) 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; CP009516; AKB76567.1; -; Genomic_DNA.
DR RefSeq; WP_048136663.1; NZ_CP009516.1.
DR AlphaFoldDB; A0A0E3SA85; -.
DR STRING; 1434110.MSHOH_0084; -.
DR GeneID; 24829199; -.
DR KEGG; mhor:MSHOH_0084; -.
DR PATRIC; fig|1434110.4.peg.94; -.
DR HOGENOM; CLU_493170_0_0_2; -.
DR OrthoDB; 52468at2157; -.
DR UniPathway; UPA00646; UER00699.
DR Proteomes; UP000033101; 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:AKB76567.1}.
FT DOMAIN 15..282
FT /note="Methyl-coenzyme M reductase alpha subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02745"
FT DOMAIN 329..461
FT /note="Methyl-coenzyme M reductase alpha subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02249"
FT BINDING 161
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 271
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000262-2"
FT MOD_RES 285
FT /note="5-methylarginine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000262-2"
SQ SEQUENCE 570 AA; 62111 MW; 056DFE6471A3CBD6 CRC64;
MAADIFSKFK KSMEVKFTQE YGSNQQSGGD ITGKTEKFLR LGPEQDARKV EMIKAGKEIA
EKRGIAFYNP MMHMGAPLGQ RAITPYTISG TDIVAEPDDL HYVNNAAMQQ MWDDIRRTCI
VGLDMAHETL EKRLGKEVTP ETINHYLEVL NHAMPGAAVV QEMMVETHPA LVDDCYVKIF
TGDDELADEV DKQFVININK MFNEEQAAQI KASIGKTTWQ AIHIPTIVSR TTDGAQTSRW
AAMQIGMSFI SAYAMCAGEA AVADLSFAAK HAALVSMGEM LPARRARGPN EPGGLSFGHL
SDIIQTSRTS EDPAKIALEV VGAGCMLYDQ IWLGSYMSGG VGFTQYATAA YTDDILDNNV
YYDVDYINDK YNGAANVGKD NKIKATLEVV KDIATESTLY GIETYEKFPT ALEDHFGGSQ
RATVLAAAAG VACALGTANA NAGLSGWYLS MYLHKEAWGR LGFFGYDLQD QCGATNVLSY
QGDEGLPDEL RGPNYPNYAM NVGHQGGYAG IAQAAHSGRG DAFTVNPLIK VCFADDLMPF
NFAEPRREFG RGAIREFVPA GERSLVIPAK
//
