ID Q6V267_9EURY Unreviewed; 252 AA.
AC Q6V267;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 22-FEB-2023, entry version 43.
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:AAQ56608.1};
OS uncultured methanogenic archaeon.
OC Archaea; Euryarchaeota; environmental samples.
OX NCBI_TaxID=198240 {ECO:0000313|EMBL:AAQ56608.1};
RN [1] {ECO:0000313|EMBL:AAQ56608.1}
RP NUCLEOTIDE SEQUENCE.
RA Nercessian O.G., Bienvenu N., Moreira D., Prieur D., Jeanthon C.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAQ56608.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15643942; DOI=10.1111/j.1462-2920.2004.00672.x;
RA Nercessian O., Bienvenu N., Moreira D., Prieur D., Jeanthon C.;
RT "Diversity of functional genes of methanogens, methanotrophs and sulfate
RT reducers in deep-sea hydrothermal environments.";
RL Environ. Microbiol. 7:118-132(2005).
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; AY354019; AAQ56608.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6V267; -.
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..41
FT /note="Methyl-coenzyme M reductase alpha subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02745"
FT DOMAIN 88..214
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:AAQ56608.1"
FT NON_TER 252
FT /evidence="ECO:0000313|EMBL:AAQ56608.1"
SQ SEQUENCE 252 AA; 27111 MW; DB27A8202A206281 CRC64;
AMQIGMSFIT AYKLCAGEAA IADFSYAAKH ADVIQMATFL PARRARGPNE PGGMFLGVMA
DVVQTSRVSD DPVEQSLEVV AAGAALFDQV WLGSYMSGGV GFTQYASASY TDDILDDFSY
YGYDYINKKY GGCNSVKPTM DVVEDIAGEV TLYALEQYDT YPALLEDHFG GSQRAAVAAA
ASGISVALAT GNSNAGLNGW YLSQIMHKEY HSRLGFYGYD LQDQCGAANS LSFRNDEGSP
LELRGPNYPN YA
//
