MCRY_METJA
ID MCRY_METJA Reviewed; 447 AA.
AC Q60390;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 125.
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; OrderedLocusNames=MJ0081;
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 -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase beta subunit
CC family. {ECO:0000305}.
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DR EMBL; L77117; AAB98061.1; -; Genomic_DNA.
DR RefSeq; WP_010869573.1; NC_000909.1.
DR AlphaFoldDB; Q60390; -.
DR SMR; Q60390; -.
DR STRING; 243232.MJ_0081; -.
DR EnsemblBacteria; AAB98061; AAB98061; MJ_0081.
DR GeneID; 1450920; -.
DR KEGG; mja:MJ_0081; -.
DR eggNOG; arCOG04860; Archaea.
DR HOGENOM; CLU_617682_0_0_2; -.
DR InParanoid; Q60390; -.
DR OMA; WALWNAY; -.
DR OrthoDB; 25508at2157; -.
DR PhylomeDB; Q60390; -.
DR UniPathway; UPA00646; UER00699.
DR Proteomes; UP000000805; Chromosome.
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 Methanogenesis; Reference proteome; Transferase.
FT CHAIN 1..447
FT /note="Methyl-coenzyme M reductase II subunit beta"
FT /id="PRO_0000147466"
FT BINDING 368
FT /ligand="coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58319"
FT /evidence="ECO:0000250|UniProtKB:P11560"
FT BINDING 370
FT /ligand="coenzyme B"
FT /ligand_id="ChEBI:CHEBI:58596"
FT /evidence="ECO:0000250|UniProtKB:P11560"
SQ SEQUENCE 447 AA; 47770 MW; B9CAE1066BE977BC CRC64;
MLHYEDRIDL YDERGKLLEE NVPLEAISPL KNPTIEKIVN DIKRSVAINL AGIENALKTG
AVGGKACFCP GRELDLPIVE NAEIIAEKIK RMVQIEEDDD TVVKLINGGK QLLLQLPSKR
LRVAADYTVS ALIGGGATVQ AIVDAFDVDM FDAPVVKTAV MGRYPQTVDF HGANIATLLG
PPVLLEGLGY GLRNIMANHI VAVTRKKTLN AVALASILEQ TAMFETGDAL GAFERLHLLG
LAFQGLNANN LTYELVKENG KDGTVGTVVA SVVERALEDG VIRPLKTMPS GFTVYEPVDW
ALWNAYAASG LVAAVIVNVG AARAAQGVAS TVLYYNDILE YETGLPSVDF GRAEGTAVGF
SFFSHSIYGG GGPGTFHGNH VVTRHSKGFA IPCAAAAMCL DAGTQMFSVE RTSALVGTVY
SAIDHLREPL KYVAEGAVEV KEKEKVI
