ID MCRB_METTM Reviewed; 443 AA. AC P11560; D9PY33; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 05-DEC-2018, entry version 123. DE RecName: Full=Methyl-coenzyme M reductase I subunit beta; DE Short=MCR I beta; DE EC=2.8.4.1; DE AltName: Full=Coenzyme-B sulfoethylthiotransferase beta; GN Name=mcrB; OrderedLocusNames=MTBMA_c15520; 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 [GENOMIC DNA]. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=2448287; DOI=10.1128/jb.170.2.568-577.1988; RA Bokranz M., Baeumner G., Allmansberger R., Ankel-Fuchs D., Klein A.; RT "Cloning and characterization of the methyl coenzyme M reductase genes RT from Methanobacterium thermoautotrophicum."; RL J. Bacteriol. 170:568-577(1988). RN [2] 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., RA Seedorf H., 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 [3] RP PROTEIN SEQUENCE OF 2-21. 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 RT Methanobacterium thermoautotrophicum strain Marburg and delta H."; RL Eur. J. Biochem. 194:871-877(1990). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS). RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=9367957; DOI=10.1126/science.278.5342.1457; RA Ermler U., Grabarse W., Shima S., Goubeaud M., Thauer R.K.; RT "Crystal structure of methyl-coenzyme M reductase: the key enzyme of RT biological methane formation."; RL Science 278:1457-1462(1997). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS). RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=11491299; DOI=10.1006/jmbi.2001.4647; RA Grabarse W., Mahlert F., Duin E.C., Goubeaud M., Shima S., RA Thauer R.K., Lamzin V., Ermler U.; RT "On the mechanism of biological methane formation: structural evidence RT for conformational changes in methyl-coenzyme M reductase upon RT substrate binding."; RL J. Mol. Biol. 309:315-330(2001). CC -!- FUNCTION: Reduction of methyl-coenzyme M (2-(methylthio) CC ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate CC to methane and a heterodisulfide. CC -!- CATALYTIC ACTIVITY: CC Reaction=coenzyme B + methyl-coenzyme M = coenzyme M-coenzyme B CC heterodisulfide + methane; Xref=Rhea:RHEA:12532, CC ChEBI:CHEBI:16183, ChEBI:CHEBI:58286, ChEBI:CHEBI:58411, CC ChEBI:CHEBI:58596; EC=2.8.4.1; CC -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; CC methane from methyl-coenzyme M: step 1/1. CC -!- SUBUNIT: Hexamer of two alpha, two beta, and two gamma chains. CC -!- DEVELOPMENTAL STAGE: There are two MCR complexes in this bacteria. CC MCR II is expressed in the early growth phase. Late growth cells CC contains mostly MCR I. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X07794; CAA30635.1; -; Genomic_DNA. DR EMBL; CP001710; ADL59131.1; -; Genomic_DNA. DR PIR; A28544; A28544. DR RefSeq; WP_013296341.1; NC_014408.1. DR PDB; 1HBM; X-ray; 1.80 A; B/E=2-443. DR PDB; 1HBN; X-ray; 1.16 A; B/E=2-443. DR PDB; 1HBO; X-ray; 1.78 A; B/E=2-443. DR PDB; 1HBU; X-ray; 1.90 A; B/E=2-443. DR PDB; 1MRO; X-ray; 1.16 A; B/E=2-443. DR PDB; 3M1V; X-ray; 1.45 A; B/E=2-443. DR PDB; 3M2R; X-ray; 1.30 A; B/E=2-443. DR PDB; 3M2U; X-ray; 1.40 A; B/E=2-443. DR PDB; 3M2V; X-ray; 1.80 A; B/E=2-443. DR PDB; 3M30; X-ray; 1.45 A; B/E=2-443. DR PDB; 3M32; X-ray; 1.35 A; B/E=2-443. DR PDB; 3POT; X-ray; 1.20 A; B/E=1-443. DR PDB; 5A0Y; X-ray; 1.10 A; B/E=1-443. DR PDB; 5G0R; X-ray; 1.25 A; B/E=1-443. DR PDBsum; 1HBM; -. DR PDBsum; 1HBN; -. DR PDBsum; 1HBO; -. DR PDBsum; 1HBU; -. DR PDBsum; 1MRO; -. DR PDBsum; 3M1V; -. DR PDBsum; 3M2R; -. DR PDBsum; 3M2U; -. DR PDBsum; 3M2V; -. DR PDBsum; 3M30; -. DR PDBsum; 3M32; -. DR PDBsum; 3POT; -. DR PDBsum; 5A0Y; -. DR PDBsum; 5G0R; -. DR ProteinModelPortal; P11560; -. DR SMR; P11560; -. DR STRING; 79929.MTBMA_c15520; -. DR EnsemblBacteria; ADL59131; ADL59131; MTBMA_c15520. DR GeneID; 9705261; -. DR KEGG; mmg:MTBMA_c15520; -. DR PATRIC; fig|79929.8.peg.1505; -. DR eggNOG; arCOG04860; Archaea. DR eggNOG; COG4054; LUCA. DR HOGENOM; HOG000225842; -. DR KO; K00401; -. DR OMA; TAMFEMG; -. DR OrthoDB; POG093Z033X; -. DR BioCyc; MMAR79929:G1GML-1527-MONOMER; -. DR BRENDA; 2.8.4.1; 7427. DR UniPathway; UPA00646; UER00699. DR EvolutionaryTrace; P11560; -. DR Proteomes; UP000000345; Chromosome. DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IDA:MENGO. 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; Complete proteome; Direct protein sequencing; KW Methanogenesis; Transferase. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2269306}. FT CHAIN 2 443 Methyl-coenzyme M reductase I subunit FT beta. FT /FTId=PRO_0000147468. FT STRAND 7 11 {ECO:0000244|PDB:5A0Y}. FT STRAND 17 23 {ECO:0000244|PDB:5A0Y}. FT HELIX 24 27 {ECO:0000244|PDB:5A0Y}. FT TURN 29 31 {ECO:0000244|PDB:5A0Y}. FT HELIX 33 44 {ECO:0000244|PDB:5A0Y}. FT STRAND 45 49 {ECO:0000244|PDB:5A0Y}. FT HELIX 50 59 {ECO:0000244|PDB:5A0Y}. FT HELIX 79 81 {ECO:0000244|PDB:5A0Y}. FT HELIX 82 93 {ECO:0000244|PDB:5A0Y}. FT STRAND 102 106 {ECO:0000244|PDB:5A0Y}. FT HELIX 107 109 {ECO:0000244|PDB:5A0Y}. FT STRAND 111 115 {ECO:0000244|PDB:5A0Y}. FT HELIX 118 122 {ECO:0000244|PDB:5A0Y}. FT STRAND 124 127 {ECO:0000244|PDB:5A0Y}. FT HELIX 129 146 {ECO:0000244|PDB:5A0Y}. FT TURN 150 152 {ECO:0000244|PDB:5A0Y}. FT HELIX 153 161 {ECO:0000244|PDB:5A0Y}. FT TURN 162 166 {ECO:0000244|PDB:5A0Y}. FT STRAND 167 169 {ECO:0000244|PDB:5A0Y}. FT STRAND 174 176 {ECO:0000244|PDB:5A0Y}. FT HELIX 182 184 {ECO:0000244|PDB:5A0Y}. FT HELIX 191 193 {ECO:0000244|PDB:5A0Y}. FT HELIX 197 203 {ECO:0000244|PDB:5A0Y}. FT TURN 204 206 {ECO:0000244|PDB:5A0Y}. FT HELIX 208 225 {ECO:0000244|PDB:5A0Y}. FT TURN 226 229 {ECO:0000244|PDB:5A0Y}. FT HELIX 231 233 {ECO:0000244|PDB:5A0Y}. FT HELIX 234 245 {ECO:0000244|PDB:5A0Y}. FT HELIX 248 250 {ECO:0000244|PDB:5A0Y}. FT HELIX 251 259 {ECO:0000244|PDB:5A0Y}. FT TURN 260 262 {ECO:0000244|PDB:5A0Y}. FT HELIX 265 278 {ECO:0000244|PDB:5A0Y}. FT STRAND 283 288 {ECO:0000244|PDB:5A0Y}. FT STRAND 291 295 {ECO:0000244|PDB:5A0Y}. FT HELIX 299 321 {ECO:0000244|PDB:5A0Y}. FT HELIX 324 326 {ECO:0000244|PDB:5A0Y}. FT HELIX 327 342 {ECO:0000244|PDB:5A0Y}. FT HELIX 347 350 {ECO:0000244|PDB:5A0Y}. FT HELIX 351 361 {ECO:0000244|PDB:5A0Y}. FT STRAND 364 368 {ECO:0000244|PDB:5A0Y}. FT HELIX 372 374 {ECO:0000244|PDB:5A0Y}. FT TURN 380 382 {ECO:0000244|PDB:5A0Y}. FT STRAND 384 389 {ECO:0000244|PDB:5A0Y}. FT HELIX 390 398 {ECO:0000244|PDB:5A0Y}. FT HELIX 408 411 {ECO:0000244|PDB:5A0Y}. FT HELIX 413 419 {ECO:0000244|PDB:5A0Y}. FT HELIX 423 426 {ECO:0000244|PDB:5A0Y}. FT HELIX 428 439 {ECO:0000244|PDB:5A0Y}. FT HELIX 440 442 {ECO:0000244|PDB:5A0Y}. SQ SEQUENCE 443 AA; 47240 MW; 1237E83E405E6D6B CRC64; MAKFEDKVDL YDDRGNLVEE QVPLEALSPL RNPAIKSIVQ GIKRTVAVNL EGIENALKTA KVGGPACKIM GRELDLDIVG NAESIAAAAK EMIQVTEDDD TNVELLGGGK RALVQVPSAR FDVAAEYSAA PLVTATAFVQ AIINEFDVSM YDANMVKAAV LGRYPQSVEY MGANIATMLD IPQKLEGPGY ALRNIMVNHV VAATLKNTLQ AAALSTILEQ TAMFEMGDAV GAFERMHLLG LAYQGMNADN LVFDLVKANG KEGTVGSVIA DLVERALEDG VIKVEKELTD YKVYGTDDLA MWNAYAAAGL MAATMVNQGA ARAAQGVSST LLYYNDLIEF ETGLPSVDFG KVEGTAVGFS FFSHSIYGGG GPGIFNGNHI VTRHSKGFAI PCVAAAMALD AGTQMFSPEA TSGLIKEVFS QVDEFREPLK YVVEAAAEIK NEI //