ID   D6NIU9_UNCAX            Unreviewed;       240 AA.
AC   D6NIU9;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-NOV-2024, entry version 19.
DE   RecName: Full=coenzyme-B sulfoethylthiotransferase {ECO:0000256|ARBA:ARBA00013271};
DE            EC=2.8.4.1 {ECO:0000256|ARBA:ARBA00013271};
DE   Flags: Fragment;
GN   Name=mcrA {ECO:0000313|EMBL:ADG63237.1};
OS   Uncultured archaeon.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=115547 {ECO:0000313|EMBL:ADG63237.1};
RN   [1] {ECO:0000313|EMBL:ADG63237.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Schulze-Makuch D., Haque S., Antonio M., Ali D., Hosein R., Song Y.C.,
RA   Yang J., Zaikova E., Beckles D.M., Guinan E., Lehto H.J., Hallam S.J.;
RT   "A Microbial Community within a Natural Asphalt Lake.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=coenzyme B + methyl-coenzyme M = methane + coenzyme M-coenzyme
CC         B heterodisulfide; 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|ARBA:ARBA00001952};
CC   -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; methane
CC       from methyl-coenzyme M: step 1/1. {ECO:0000256|ARBA:ARBA00005149}.
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; GU447206; ADG63237.1; -; Genomic_DNA.
DR   AlphaFoldDB; D6NIU9; -.
DR   UniPathway; UPA00646; UER00699.
DR   GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
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; 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; IPR015823; Me_CoM_Rdtase_asu_N_sub2.
DR   InterPro; IPR009024; Me_CoM_Rdtase_Fd-like_fold.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 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   Methanogenesis {ECO:0000256|ARBA:ARBA00022994};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Nickel {ECO:0000256|ARBA:ARBA00022596}.
FT   DOMAIN          1..34
FT                   /note="Methyl-coenzyme M reductase alpha subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02745"
FT   DOMAIN          82..208
FT                   /note="Methyl-coenzyme M reductase alpha subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02249"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADG63237.1"
FT   NON_TER         240
FT                   /evidence="ECO:0000313|EMBL:ADG63237.1"
SQ   SEQUENCE   240 AA;  26031 MW;  EB5C52BB0FFB2A22 CRC64;
     FINAYKMCAG ESATGEFAFM AKHASVVQTS NYMPVRRARA QNELGGLPLG VCDDMTRSPA
     LFPNDPVRAE LEAIAAAALL YDQLWFGTYM SGGVGFTQYA SATYTDNILE DFCYKADEIA
     VDMFGERCAA EPTMENIEKL VRAENDYTLT QYDAYPTTAE THFGGSVRAC CTSAGCSTAV
     VSATGCAQCG LNAWGLAQLL HYGTVGRLGF YGYDLQDQCT SSTSFTYRSD EGLPFEMRGV
//