MCRB_METJA
ID MCRB_METJA Reviewed; 447 AA.
AC Q58252;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Methyl-coenzyme M reductase I subunit beta;
DE Short=MCR I beta;
DE EC=2.8.4.1 {ECO:0000250|UniProtKB:P11560};
DE AltName: Full=Coenzyme-B sulfoethylthiotransferase beta;
GN Name=mcrB; OrderedLocusNames=MJ0842;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {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; L77117; AAB98847.1; -; Genomic_DNA.
DR AlphaFoldDB; Q58252; -.
DR SMR; Q58252; -.
DR STRING; 243232.MJ_0842; -.
DR EnsemblBacteria; AAB98847; AAB98847; MJ_0842.
DR KEGG; mja:MJ_0842; -.
DR eggNOG; arCOG04860; Archaea.
DR HOGENOM; CLU_617682_0_0_2; -.
DR InParanoid; Q58252; -.
DR OMA; TAMFEMG; -.
DR PhylomeDB; Q58252; -.
DR UniPathway; UPA00646; UER00699.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.840.10; -; 1.
DR Gene3D; 3.30.70.470; -; 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 Pfam; PF02241; MCR_beta; 1.
DR Pfam; PF02783; MCR_beta_N; 1.
DR PIRSF; PIRSF000263; Meth_CoM_rd_beta; 1.
DR SUPFAM; SSF48081; SSF48081; 1.
DR SUPFAM; SSF55088; SSF55088; 1.
DR TIGRFAMs; TIGR03257; met_CoM_red_bet; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methanogenesis; Reference proteome; Transferase.
FT CHAIN 1..447
FT /note="Methyl-coenzyme M reductase I subunit beta"
FT /id="PRO_0000147465"
FT BINDING 371
FT /ligand="coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58319"
FT /evidence="ECO:0000250|UniProtKB:P11560"
FT BINDING 373
FT /ligand="coenzyme B"
FT /ligand_id="ChEBI:CHEBI:58596"
FT /evidence="ECO:0000250|UniProtKB:P11560"
SQ SEQUENCE 447 AA; 47789 MW; 52C76BB2C4C425E7 CRC64;
MIPMVKYKDT INLYDEKGKL VEENVPLEAI SPLHNPTIQK LVKDVKRTVA VNLAGIENAL
RTGQVGGKGC MIKGRELDLP IVENAETIAE YVEKVVRVSE DDDTSIKLIN DGKQMAVQIP
SKRLDVAAEY SVSVLVTAQA LKEAIIRTFD VDIFDAPMVH AAVLGGYPHE VTMKGSNIAA
LLGSPLSLEG PGYALRNIMA NHFVACTKKN VMNAVAFAAI MEQTAMFEMG DAVGLFERLH
LLGLAYQGLN ADNLVIDLVK ANGKNGTVGT VVASVVERAL EDGVIKEDKT LPSGFKLYKP
VDVAKWNAYA AAGLVAAAIV NCGAARAAQN IASTILYYND ILEYETGLPG VDFGRAEGTA
VGFSFFSHSI YGGGGPGIFN GNHIVTRHSK GFAIPPVAAA MCLDAGTQMF SPERTSALVG
TVFSAIDEFR EPLKYVIKGA LEVKDKI
