ID M1P893_METMZ Unreviewed; 570 AA.
AC M1P893;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=MmTuc01_1281 {ECO:0000313|EMBL:AGF96667.1};
OS Methanosarcina mazei Tuc01.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=1236903 {ECO:0000313|EMBL:AGF96667.1, ECO:0000313|Proteomes:UP000011718};
RN [1] {ECO:0000313|EMBL:AGF96667.1, ECO:0000313|Proteomes:UP000011718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuc01 {ECO:0000313|EMBL:AGF96667.1,
RC ECO:0000313|Proteomes:UP000011718};
RX PubMed=23704185;
RA Assis das Gracas D., Thiago Juca Ramos R., Vieira Araujo A.C., Zahlouth R.,
RA Ribeiro Carneiro A., Souza Lopes T., Azevedo Barauna R., Azevedo V.,
RA Cruz Schneider M.P., Pellizari V.H., Silva A.;
RT "Complete Genome of a Methanosarcina mazei Strain Isolated from Sediment
RT Samples from an Amazonian Flooded Area.";
RL Genome Announc. 1:E00271-13(2013).
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; CP004144; AGF96667.1; -; Genomic_DNA.
DR AlphaFoldDB; M1P893; -.
DR KEGG; mmaz:MmTuc01_1281; -.
DR HOGENOM; CLU_493170_0_0_2; -.
DR BioCyc; MMAZ1236903:G139K-1225-MONOMER; -.
DR UniPathway; UPA00646; UER00699.
DR Proteomes; UP000011718; 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 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; 61943 MW; 46C1E6DF6BAF6F86 CRC64;
MAADIFSKFK KSMEVKFTQE YGSNQQTGGD ITGKTEKFLR LGPEQDARKA EMIKAGKEIA
EKRGIAFYNP MMHSGAPLGQ RAITPYTISG TDIVAEPDDL HYVNNAAMQQ MWDDIRRTCI
VGLDMAHETL EKRLGKEVTP ETINHYLEVL NHAMPGAAVV QEMMVETHPA LVDDCYVKVF
TGDDELADEI DKQYVININK MFSEEQAAQI KASIGKTSWQ AIHIPTIVSR TTDGAQTSRW
AAMQIGMSFI SAYAMCAGEA AVADLSFAAK HAALVSMGEM LPARRARGPN EPGGLSFGHL
SDIVQTSRTS EDPAKVALEV VGAGCMLYDQ IWLGSYMSGG VGFTQYATAA YTDDILDNNV
YYDVDYINDK YNGAANLGTD NKVKATLDVV KDIATESTLY GIETYEKFPT ALEDHFGGSQ
RATVLAAAAG VACALGTANA NAGLSGWYLS MYLHKEAWGR LGFFGYDLQD QCGATNVLSY
QGDEGLPDEL RGPNYPNYAM NVGHQGGYAG IAQAAHAGRG DAFTVNPLIK VCFADDLMPF
NFAEPRREFG RGAIREFVPA GERSLVIPAK
//
