MCRY_METTH
ID MCRY_METTH Reviewed; 443 AA.
AC P21111; O27204;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Methyl-coenzyme M reductase II subunit beta {ECO:0000303|PubMed:2269306};
DE Short=MCR II beta {ECO:0000303|PubMed:2269306};
DE EC=2.8.4.1 {ECO:0000269|PubMed:2269306};
DE AltName: Full=Coenzyme-B sulfoethylthiotransferase beta;
GN Name=mrtB; OrderedLocusNames=MTH_1132;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=7929010; DOI=10.1128/jb.176.20.6384-6391.1994;
RA Pihl T.D., Sharma S., Reeve J.N.;
RT "Growth phase-dependent transcription of the genes that encode the two
RT methyl coenzyme M reductase isoenzymes and N5-
RT methyltetrahydromethanopterin:coenzyme M methyltransferase in
RT Methanobacterium thermoautotrophicum delta H.";
RL J. Bacteriol. 176:6384-6391(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-146.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=2654933; DOI=10.1073/pnas.86.9.3031;
RA Reeve J.N., Beckler G.S., Cram D.S., Hamilton P.T., Brown J.W.,
RA Krzycki J.A., Kolodziej A.F., Alex L., Orme-Johnson W.H., Walsh C.T.;
RT "A hydrogenase-linked gene in Methanobacterium thermoautotrophicum strain
RT delta H encodes a polyferredoxin.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:3031-3035(1989).
RN [4]
RP PROTEIN SEQUENCE OF 2-20, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=2269306; DOI=10.1111/j.1432-1033.1990.tb19481.x;
RA Rospert S., Linder D., Ellermann J., Thauer R.K.;
RT "Two genetically distinct methyl-coenzyme M reductases in Methanobacterium
RT thermoautotrophicum strain Marburg and delta H.";
RL Eur. J. Biochem. 194:871-877(1990).
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:0000269|PubMed:2269306}.
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:0000269|PubMed:2269306};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12533;
CC Evidence={ECO:0000305|PubMed:2269306};
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:0000305|PubMed:2269306}.
CC -!- SUBUNIT: MCR is a hexamer of two alpha, two beta, and two gamma chains,
CC forming a dimer of heterotrimers. {ECO:0000269|PubMed:2269306}.
CC -!- DEVELOPMENTAL STAGE: There are two MCR complexes in this bacteria. MCR
CC II is expressed in the early growth phase. Late growth cells contain
CC mostly MCR I. {ECO:0000250|UniProtKB:P11560}.
CC -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase beta subunit
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB85621.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U09990; AAA73436.1; -; Genomic_DNA.
DR EMBL; AE000666; AAB85621.1; ALT_INIT; Genomic_DNA.
DR EMBL; J04540; AAB02353.1; -; Genomic_DNA.
DR PIR; G69017; G69017.
DR PIR; T45147; T45147.
DR RefSeq; WP_048060974.1; NC_000916.1.
DR AlphaFoldDB; P21111; -.
DR SMR; P21111; -.
DR IntAct; P21111; 1.
DR STRING; 187420.MTH_1132; -.
DR EnsemblBacteria; AAB85621; AAB85621; MTH_1132.
DR GeneID; 1471540; -.
DR KEGG; mth:MTH_1132; -.
DR PATRIC; fig|187420.15.peg.1109; -.
DR HOGENOM; CLU_617682_0_0_2; -.
DR OMA; WALWNAY; -.
DR BioCyc; MetaCyc:MRTBMAUTO-MON; -.
DR UniPathway; UPA00646; UER00699.
DR Proteomes; UP000005223; 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 1: Evidence at protein level;
KW Direct protein sequencing; Methanogenesis; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2269306"
FT CHAIN 2..443
FT /note="Methyl-coenzyme M reductase II subunit beta"
FT /id="PRO_0000147469"
FT BINDING 367
FT /ligand="coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58319"
FT /evidence="ECO:0000250|UniProtKB:D9PXZ6"
FT BINDING 369
FT /ligand="coenzyme B"
FT /ligand_id="ChEBI:CHEBI:58596"
FT /evidence="ECO:0000250|UniProtKB:D9PXZ6"
FT CONFLICT 294
FT /note="Y -> I (in Ref. 1; AAA73436)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 47134 MW; 462293DE946E994E CRC64;
MPMYEDRIDL YGADGKLLEE DVPLEAVSPL KNPTIANLVS DVKRSVAVNL AGIEGSLKKA
ALGGKSNFIP GREVELPIVE NAEAIAEKVK RLVQTSEDDD TNIRLINNGQ QILVQVPTTR
MGVAADYTVS ALVTGAAVVQ AIIDEFDVDM FDANAVKTAV MGRYPQTVDF TGANLSTLLG
PPVLLEGLGY GLRNIMANHV VAITRKNTLN ASALSSILEQ TAMFETGDAV GAFERMHLLG
LAYQGLNANN LLFDLVKENS KGTVGTVIAS LVERAIEDRV IKVASEMKSG YKMYEPADWA
LWNAYAATGL LAATIVNVGA ARAAQGVAST VLYYNDILEY ETGLPGVDFG RAMGTAVGFS
FFSHSIYGGG GPGIFHGNHV VTRHSKGFAL PCVAAAMCLD AGTQMFSVEK TSGLIGSVYS
EIDYFREPIV NVAKGAAEIK DQL
