ID MCRY_METFV Reviewed; 443 AA.
AC Q49171; E3GYZ8; Q49177;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Methyl-coenzyme M reductase II subunit beta;
DE Short=MCR II beta;
DE EC=2.8.4.1 {ECO:0000250|UniProtKB:P11560};
DE AltName: Full=Coenzyme-B sulfoethylthiotransferase beta;
GN Name=mrtB; Synonyms=mcrIIB; OrderedLocusNames=Mfer_0731;
OS Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanothermaceae; Methanothermus.
OX NCBI_TaxID=523846;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S;
RX PubMed=8177216; DOI=10.1007/bf00280317;
RA Lehmacher A., Klenk H.-P.;
RT "Characterization and phylogeny of mcrII, a gene cluster encoding an
RT isoenzyme of methyl coenzyme M reductase from hyperthermophilic
RT Methanothermus fervidus.";
RL Mol. Gen. Genet. 243:198-206(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S;
RX PubMed=21304736; DOI=10.4056/sigs.1283367;
RA Anderson I., Djao O.D., Misra M., Chertkov O., Nolan M., Lucas S.,
RA Lapidus A., Del Rio T.G., Tice H., Cheng J.F., Tapia R., Han C.,
RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Brambilla E., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Sikorski J., Spring S., Rohde M.,
RA Eichinger K., Huber H., Wirth R., Goker M., Detter J.C., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Methanothermus fervidus type strain (V24S).";
RL Stand. Genomic Sci. 3:315-324(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125.
RA Steigerwald V.J., Stroup D., Hennigan A.N., Pihl T.D., Reeve J.N.;
RL Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P11560}.
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:0000250|UniProtKB:P11560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12533;
CC Evidence={ECO:0000250|UniProtKB:P11560};
CC -!- COFACTOR:
CC Name=coenzyme F430; Xref=ChEBI:CHEBI:60540;
CC Evidence={ECO:0000250|UniProtKB:P11560};
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:0000250|UniProtKB:P11560};
CC -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; methane
CC from methyl-coenzyme M: step 1/1. {ECO:0000250|UniProtKB:P11560}.
CC -!- SUBUNIT: MCR is a hexamer of two alpha, two beta, and two gamma chains,
CC forming a dimer of heterotrimers. {ECO:0000250|UniProtKB:P11560}.
CC -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase beta subunit
CC family. {ECO:0000305}.
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DR EMBL; X70765; CAA50041.1; -; Genomic_DNA.
DR EMBL; CP002278; ADP77530.1; -; Genomic_DNA.
DR EMBL; M99219; AAA73384.1; -; Genomic_DNA.
DR PIR; S43899; S43899.
DR RefSeq; WP_013413808.1; NC_014658.1.
DR AlphaFoldDB; Q49171; -.
DR SMR; Q49171; -.
DR STRING; 523846.Mfer_0731; -.
DR GeneID; 9962461; -.
DR KEGG; mfv:Mfer_0731; -.
DR HOGENOM; CLU_617682_0_0_2; -.
DR OrthoDB; 52873at2157; -.
DR UniPathway; UPA00646; UER00699.
DR Proteomes; UP000002315; Chromosome.
DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:UniProtKB-EC.
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; IPR015823; Me_CoM_Rdtase_asu_N_sub2.
DR InterPro; IPR003179; Me_CoM_Rdtase_bsu.
DR InterPro; IPR022679; Me_CoM_Rdtase_bsu_C.
DR InterPro; IPR022680; Me_CoM_Rdtase_bsu_N.
DR InterPro; IPR009024; Me_CoM_Rdtase_Fd-like_fold.
DR NCBIfam; TIGR03257; met_CoM_red_bet; 1.
DR Pfam; PF02241; MCR_beta; 1.
DR Pfam; PF02783; MCR_beta_N; 1.
DR PIRSF; PIRSF000263; Meth_CoM_rd_beta; 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 Methanogenesis; Reference proteome; Transferase.
FT CHAIN 1..443
FT /note="Methyl-coenzyme M reductase II subunit beta"
FT /id="PRO_0000147464"
FT BINDING 367
FT /ligand="coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58319"
FT /evidence="ECO:0000250|UniProtKB:P11560"
FT BINDING 369
FT /ligand="coenzyme B"
FT /ligand_id="ChEBI:CHEBI:58596"
FT /evidence="ECO:0000250|UniProtKB:P11560"
SQ SEQUENCE 443 AA; 47447 MW; FEAA6DDD20A262E6 CRC64;
MAIYEDKIDL YDANGKLLDE NVPLEAISPL KNPTIGKIVN DVKRSVAVNL AGIENSLKKA
ALGGKANFIP GRELDLDIVE NAEIIAEKIK KMVQVDENDD TNVKMINNGQ QLLVQVPTIR
IERAADYTVS TLVAGAATIQ AIIDTFDVDM FDASTVKTAV LGRYPQTVDF TGANVAAMLS
PPVLLEGLGY GLRNILTNHI VATTKKNTLN AAALSSILEQ TAMFETGDAV GAFERLHLLG
LAYQGLNADN LVYDLVKENK KGTVGTVIAS LVERAIEDKV IKVSKEMPSG FRVYEPIDWA
LWNAYAAAGL LAATIVNIGA ARAAQGVAST VLYYNDILEY ETGLPGVDFG RAEGTAVGFS
FFSHSIYGGG GPGIFHGNHV VTRHSKGFAL PCVAAAMSLD AGTQMFSPER TSGLVGQVYS
EIDYFREPIK YVAEGAAKIK NKI
//
