ID MCRB_METTM Reviewed; 443 AA. AC P11560; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 01-MAY-2007, entry version 53. DE Methyl-coenzyme M reductase I subunit beta (EC 2.8.4.1) (Coenzyme-B DE sulfoethylthiotransferase beta) (MCR I beta). GN Name=mcrB; OS Methanobacterium thermoautotrophicum (strain Marburg / DSM 2133). OC Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; OC Methanobacteriaceae; Methanothermobacter. OX NCBI_TaxID=79929; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=88115150; PubMed=2448287; 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 PROTEIN SEQUENCE OF 2-21. RX MEDLINE=91099370; PubMed=2269306; 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 [3] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS). RX MEDLINE=98035783; 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 [4] RP X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS). RX MEDLINE=21383388; 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 an heterodisulfide. CC -!- CATALYTIC ACTIVITY: 2-(methylthio)ethanesulfonate (methyl-CoM) + CC N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) = CoM- CC S-S-CoB + methane. CC -!- COFACTOR: Binds 2 coenzyme F430 noncovalently per hexamer. CC Coenzyme F430 is a yellow nickel porphinoid. CC -!- PATHWAY: Methanogenesis; last step. 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 PIR; A28544; A28544. DR PDB; 1HBM; X-ray; B/E=-. DR PDB; 1HBN; X-ray; B/E=-. DR PDB; 1HBO; X-ray; B/E=-. DR PDB; 1HBU; X-ray; B/E=-. DR PDB; 1MRO; X-ray; B/E=-. DR SMR; P11560; 2-443. DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:EC. DR InterPro; IPR013804; MCR_a/b_chain_a-bundle. DR InterPro; IPR008924; MCR_a/b_chain_C. DR InterPro; IPR003179; MCR_beta. DR InterPro; IPR009024; MCR_fer_like. DR Gene3D; G3DSA:1.20.840.10; MCR_a/b_chain_a-bundle; 2. DR Pfam; PF02241; MCR_beta; 1. DR Pfam; PF02783; MCR_beta_N; 1. DR PIRSF; PIRSF000263; Meth_CoM_rd_beta; 1. KW 3D-structure; Direct protein sequencing; Methanogenesis; Transferase. FT INIT_MET 1 1 Removed. FT CHAIN 2 443 Methyl-coenzyme M reductase I subunit FT beta. FT /FTId=PRO_0000147468. FT STRAND 7 11 FT TURN 13 14 FT STRAND 17 23 FT HELIX 24 27 FT TURN 29 31 FT HELIX 33 44 FT STRAND 45 49 FT HELIX 50 59 FT TURN 60 60 FT TURN 65 66 FT TURN 70 71 FT TURN 78 78 FT HELIX 79 81 FT HELIX 82 93 FT TURN 97 98 FT STRAND 102 106 FT HELIX 107 109 FT TURN 110 110 FT STRAND 111 115 FT HELIX 118 122 FT TURN 123 123 FT TURN 128 128 FT HELIX 129 146 FT TURN 147 147 FT TURN 150 152 FT HELIX 153 161 FT TURN 162 166 FT TURN 171 172 FT STRAND 175 176 FT HELIX 182 184 FT TURN 188 189 FT HELIX 191 193 FT HELIX 197 203 FT TURN 204 206 FT HELIX 208 225 FT TURN 226 229 FT HELIX 231 233 FT HELIX 234 245 FT HELIX 248 250 FT HELIX 251 259 FT TURN 260 262 FT HELIX 265 278 FT TURN 279 280 FT STRAND 283 288 FT TURN 289 290 FT STRAND 291 295 FT HELIX 299 321 FT TURN 322 322 FT HELIX 324 326 FT HELIX 327 342 FT HELIX 347 350 FT HELIX 351 361 FT TURN 362 363 FT HELIX 372 374 FT TURN 377 378 FT TURN 380 382 FT HELIX 390 399 FT HELIX 408 411 FT HELIX 413 419 FT TURN 420 421 FT HELIX 423 426 FT HELIX 428 439 FT TURN 440 443 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 //