MCRB_METBF
ID MCRB_METBF Reviewed; 434 AA.
AC P07955; Q46E21;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Methyl-coenzyme M reductase subunit beta;
DE EC=2.8.4.1 {ECO:0000250|UniProtKB:P11560};
DE AltName: Full=Coenzyme-B sulfoethylthiotransferase beta;
GN Name=mcrB; OrderedLocusNames=Mbar_A0897;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3502709; DOI=10.1093/nar/15.10.4350;
RA Bokranz M., Klein A.;
RT "Nucleotide sequence of the methyl coenzyme M reductase gene cluster from
RT Methanosarcina barkeri.";
RL Nucleic Acids Res. 15:4350-4351(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
RN [3] {ECO:0007744|PDB:1E6Y}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH COENZYME F430;
RP COENZYME B; COENZYME M AND MCR SUBUNITS ALPHA AND GAMMA, FUNCTION,
RP COFACTOR, AND SUBUNIT.
RC STRAIN=Fusaro / DSM 804;
RX PubMed=11023796; DOI=10.1006/jmbi.2000.4136;
RA Grabarse W., Mahlert F., Shima S., Thauer R.K., Ermler U.;
RT "Comparison of three methyl-coenzyme M reductases from phylogenetically
RT distant organisms: unusual amino acid modification, conservation and
RT adaptation.";
RL J. Mol. Biol. 303:329-344(2000).
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:0000305|PubMed:11023796}.
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:0000269|PubMed:11023796};
CC Note=Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme
CC F430 is a yellow nickel porphinoid (PubMed:11023796). Methyl-coenzyme-M
CC reductase is activated when the enzyme-bound coenzyme F430 is reduced
CC to the Ni(I) oxidation state (By similarity).
CC {ECO:0000250|UniProtKB:P11560, ECO:0000269|PubMed:11023796};
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:0000269|PubMed:11023796}.
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; Y00158; CAA68353.1; -; Genomic_DNA.
DR EMBL; CP000099; AAZ69871.1; -; Genomic_DNA.
DR PIR; A29525; A29525.
DR RefSeq; WP_011305920.1; NC_007355.1.
DR PDB; 1E6Y; X-ray; 1.60 A; B/E=2-434.
DR PDBsum; 1E6Y; -.
DR AlphaFoldDB; P07955; -.
DR SMR; P07955; -.
DR STRING; 269797.Mbar_A0897; -.
DR PRIDE; P07955; -.
DR EnsemblBacteria; AAZ69871; AAZ69871; Mbar_A0897.
DR GeneID; 3625942; -.
DR KEGG; mba:Mbar_A0897; -.
DR eggNOG; arCOG04860; Archaea.
DR HOGENOM; CLU_617682_0_0_2; -.
DR OMA; TAMFEMG; -.
DR OrthoDB; 25508at2157; -.
DR BRENDA; 2.8.4.1; 3250.
DR UniPathway; UPA00646; UER00699.
DR EvolutionaryTrace; P07955; -.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methanogenesis; Transferase.
FT CHAIN 1..434
FT /note="Methyl-coenzyme M reductase subunit beta"
FT /id="PRO_0000147462"
FT BINDING 365
FT /ligand="coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58319"
FT /evidence="ECO:0000269|PubMed:11023796,
FT ECO:0007744|PDB:1E6Y"
FT BINDING 367
FT /ligand="coenzyme B"
FT /ligand_id="ChEBI:CHEBI:58596"
FT /evidence="ECO:0000269|PubMed:11023796,
FT ECO:0007744|PDB:1E6Y"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1E6Y"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:1E6Y"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 30..41
FT /evidence="ECO:0007829|PDB:1E6Y"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:1E6Y"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:1E6Y"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:1E6Y"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:1E6Y"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 126..142
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:1E6Y"
FT TURN 159..163
FT /evidence="ECO:0007829|PDB:1E6Y"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1E6Y"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:1E6Y"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 205..222
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 229..243
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 248..256
FT /evidence="ECO:0007829|PDB:1E6Y"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 262..275
FT /evidence="ECO:0007829|PDB:1E6Y"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:1E6Y"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 297..319
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 325..340
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 349..359
FT /evidence="ECO:0007829|PDB:1E6Y"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:1E6Y"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:1E6Y"
FT STRAND 382..387
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 388..397
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 406..417
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 421..424
FT /evidence="ECO:0007829|PDB:1E6Y"
FT HELIX 426..431
FT /evidence="ECO:0007829|PDB:1E6Y"
SQ SEQUENCE 434 AA; 45421 MW; A85044187FB78CB9 CRC64;
MSDTVDIYDD RGKLLESNVD IMSLAPTRNA AIQSIIMDTK RSVAVNLAGI QGALASGKMG
GKGRQILGRG LNYDIVGNAD AIAENVKKLV QVDEGDDTNV IKVKGGKSLL IQSPKSRIIA
GADFMSATTV GAAAVTQTIM DMFGTDPYDA PIVKSAVWGS YPQTMDLMGG QVQGILSIPQ
NNEGLGFSLR NIMANHVAAI SNRNAMNASA LSSIYEQSGI FEMGGAVGMF ERHQLLGLAY
QGLNANNLLY DIVKENGKDG TIGTVIESVV RRAIEAGIIS VDKTAPSGYN FYKANDVPKW
NACAAVGTLA ATLVNCGAGR AAQNVSSTLL YFNDILEKET GLPGCDYGKV EGTAVGFSFF
SHSIYGGGGP GVFNGNHVVT RHSRGFAIPC VCAAVALDAG TQMFSIESTS GLIGDVFGAI
PEFREPIKAV AGVL
