MCRY_METTM
ID MCRY_METTM Reviewed; 443 AA.
AC D9PXZ6;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
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 {ECO:0000255|PIRNR:PIRNR000263};
GN Name=mrtB {ECO:0000312|EMBL:ADL59094.1};
GN OrderedLocusNames=MTBMA_c15150 {ECO:0000312|EMBL:ADL59094.1};
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
RN [2]
RP PROTEIN SEQUENCE OF 2-15, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
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).
RN [3] {ECO:0007744|PDB:5A8R}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH COENZYME F430;
RP COENZYME B; COENZYME M AND MCR SUBUNITS ALPHA AND GAMMA, COFACTOR, AND
RP SUBUNIT.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=27467699; DOI=10.1002/anie.201603882;
RA Wagner T., Kahnt J., Ermler U., Shima S.;
RT "Didehydroaspartate Modification in Methyl-CoenzymeM Reductase Catalyzing
RT Methane Formation.";
RL Angew. Chem. Int. Ed. Engl. 55:10630-10633(2016).
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:0000269|PubMed:27467699};
CC Note=Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme
CC F430 is a yellow nickel porphinoid. {ECO:0000269|PubMed:27467699};
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 ECO:0000269|PubMed:27467699}.
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:0000269|PubMed:2269306}.
CC -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase beta subunit
CC family. {ECO:0000305}.
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DR EMBL; CP001710; ADL59094.1; -; Genomic_DNA.
DR RefSeq; WP_013296305.1; NC_014408.1.
DR PDB; 5A8R; X-ray; 2.15 A; B/E/H/K=1-443.
DR PDBsum; 5A8R; -.
DR AlphaFoldDB; D9PXZ6; -.
DR SMR; D9PXZ6; -.
DR STRING; 79929.MTBMA_c15150; -.
DR EnsemblBacteria; ADL59094; ADL59094; MTBMA_c15150.
DR GeneID; 9705224; -.
DR KEGG; mmg:MTBMA_c15150; -.
DR PATRIC; fig|79929.8.peg.1468; -.
DR HOGENOM; CLU_617682_0_0_2; -.
DR OMA; WALWNAY; -.
DR OrthoDB; 25508at2157; -.
DR UniPathway; UPA00646; UER00699.
DR Proteomes; UP000000345; 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 3D-structure; Direct protein sequencing; Methanogenesis; 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_0000446663"
FT BINDING 367
FT /ligand="coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58319"
FT /evidence="ECO:0000269|PubMed:27467699,
FT ECO:0007744|PDB:5A8R"
FT BINDING 369
FT /ligand="coenzyme B"
FT /ligand_id="ChEBI:CHEBI:58596"
FT /evidence="ECO:0000269|PubMed:27467699,
FT ECO:0007744|PDB:5A8R"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:5A8R"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:5A8R"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:5A8R"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:5A8R"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:5A8R"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:5A8R"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 129..146
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 150..161
FT /evidence="ECO:0007829|PDB:5A8R"
FT TURN 162..166
FT /evidence="ECO:0007829|PDB:5A8R"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:5A8R"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:5A8R"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 208..225
FT /evidence="ECO:0007829|PDB:5A8R"
FT TURN 226..229
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:5A8R"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 264..277
FT /evidence="ECO:0007829|PDB:5A8R"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:5A8R"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 299..321
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 327..342
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 351..361
FT /evidence="ECO:0007829|PDB:5A8R"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:5A8R"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:5A8R"
FT STRAND 384..389
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 390..399
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 408..419
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 423..426
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 428..439
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:5A8R"
SQ SEQUENCE 443 AA; 47000 MW; 774FE3020E0CE22A CRC64;
MPMYEDRIDL YGADGKLLEE DVPLEAISPL KNPTIANLVS DVKRSVAVNL AGIEGSLRKA
ALGGKSNFIP GREVELPIVE NAEAIAEKVK KLVQTSEDDD TNIRLINNGQ QILVQVPTTR
MGVAADYTVS ALVTGAAVVQ AIIDEFDVDM FDANAVKTAV MGRYPQTVDF TGANLSTLLG
PPVLLEGLGY GLRNIMANHV VAITRKNTLN ASALSSILEQ TAMFETGDAV GAFERMHLLG
LAYQGLNANN LLFDLVKENG KGTVGTVIAS LVERAVEDGV VKVAREMNSG YKVYEPADWA
LWNAYAATGL LAATIVNVGA ARAAQGVAST VLYYNDILEY ETGLPGVDFG RAMGTAVGFS
FFSHSIYGGG GPGIFHGNHV VTRHSKGFAL PCVAAAMCLD AGTQMFSVEK TSGLIGSVYS
EIDYFREPIV NVAKGAAEVK DQL
