ID Q6L779_9EURY Unreviewed; 216 AA.
AC Q6L779;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 22-FEB-2023, entry version 49.
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:BAD21108.1};
OS uncultured Methanomicrobiales archaeon.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; environmental samples.
OX NCBI_TaxID=183760 {ECO:0000313|EMBL:BAD21108.1};
RN [1] {ECO:0000313|EMBL:BAD21108.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15240282; DOI=10.1128/AEM.70.7.4048-4052.2004;
RA Shigematsu T., Tang Y., Kobayashi T., Kawaguchi H., Morimura S., Kida K.;
RT "Effect of dilution rate on metabolic pathway shift between aceticlastic
RT and nonaceticlastic methanogenesis in chemostat cultivation.";
RL Appl. Environ. Microbiol. 70:4048-4052(2004).
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|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; AB158525; BAD21104.1; -; mRNA.
DR EMBL; AB158529; BAD21108.1; -; mRNA.
DR AlphaFoldDB; Q6L779; -.
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 2: Evidence at transcript level;
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..215
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:BAD21108.1"
FT NON_TER 216
FT /evidence="ECO:0000313|EMBL:BAD21108.1"
SQ SEQUENCE 216 AA; 23501 MW; 269533B066B01AB5 CRC64;
FIGAYRMCAG EAAVADLAFA AKHAGVIQMA THLPARRARG PNEPGGLAFG LFSDIIQANR
KYPNDPAKAS LEVVGAGTML YDQIWLGSYM SGGVGFTQYA TAAYTDNILD EFTYYGMDYI
KDKYKVDWKN PSPKDRVKPT QEVVNDITTE VALNAMEQYE QYPTMMEDHF GGSQRAGVIA
AACGLSTSIA TGNSNAGLNA WYLSMLLHKE GWSRLG
//
