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Database: UniProt
Entry: R7Q044_9EURY
LinkDB: R7Q044_9EURY
Original site: R7Q044_9EURY 
ID   R7Q044_9EURY            Unreviewed;       554 AA.
AC   R7Q044;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=coenzyme-B sulfoethylthiotransferase {ECO:0000256|ARBA:ARBA00013271};
DE            EC=2.8.4.1 {ECO:0000256|ARBA:ARBA00013271};
GN   ORFNames=BN463_00379 {ECO:0000313|EMBL:CDF30177.1};
OS   Methanoculleus sp. CAG:1088.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=1262903 {ECO:0000313|EMBL:CDF30177.1, ECO:0000313|Proteomes:UP000018376};
RN   [1] {ECO:0000313|EMBL:CDF30177.1, ECO:0000313|Proteomes:UP000018376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:1088 {ECO:0000313|Proteomes:UP000018376};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDF30177.1}.
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DR   EMBL; CBKQ010000013; CDF30177.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7Q044; -.
DR   UniPathway; UPA00646; UER00699.
DR   Proteomes; UP000018376; Unassembled WGS sequence.
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; 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   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          7..271
FT                   /note="Methyl-coenzyme M reductase alpha subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02745"
FT   DOMAIN          319..446
FT                   /note="Methyl-coenzyme M reductase alpha subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02249"
SQ   SEQUENCE   554 AA;  61069 MW;  F2DB4A4855A11C16 CRC64;
     MAGKANEKLF LEACKKKFKE DPTSMETKYY CYGGWKQSKS KVEFQKEAME IAKKRGFPMM
     NEDIGVPLGQ RSWMPYQLSH TDIFVEPDDL HCINNPAIQQ AWDDIRRTVL VGLDSPHQTI
     ERRLGKEVTP ETINAYLETV NHTMPGGAVV QEHMAECNPA LVYDSYVKVF SGDDELIDEL
     DPRFVIDINK NFPKDQAEKL KKAIGKTVMQ AVRVPTMVGR VMDGATVSRH AAMQISMAFI
     SSYKLAAGEA AIADFAYSAK HMSINMGSMM PARRVRGPNE PGGITFGFLD DMVQSDRVYP
     DDPARAVLET VALGAIIYDQ VYLGGYMSGG VGFTQYATAA YTDNILEDYV YHAVDVINDR
     YGGFCGVAPD DYDKQLKLGD EISSYALEMY ERYPAVMETH FGGSQRATVT AASTGIAGAM
     ATGVADNGLN LWYQSMLQHK ERTGRLGFYG FDLQDQCGSA NSYAYRSDEG LPMEVRGPNY
     PNYAMNVGHL SGYAGIPKAA HAARGDAFVA SPLIKVAFSD KSLIFDFANI TKEIGRGGLR
     EFQPAGERTA VIKG
//
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