ID MCRB_METTM STANDARD; PRT; 442 AA. AC P11560; DT 01-OCT-1989 (Rel. 12, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Methyl-coenzyme M reductase I beta subunit (EC 2.8.4.1) (Coenzyme-B DE sulfoethylthiotransferase beta) (MCR I beta). GN MCRB. OS Methanobacterium thermoautotrophicum (strain Marburg / DSM 2133). OC Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; OC Methanobacteriaceae; Methanothermobacter. OX NCBI_TaxID=79929; RN [1] RP SEQUENCE FROM N.A. 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 RT genes from Methanobacterium thermoautotrophicum."; RL J. Bacteriol. 170:568-577(1988). RN [2] RP SEQUENCE OF 1-20. 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; 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; 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; -. DR PIR; A28544; A28544. DR PDB; 1MRO; 11-NOV-98. DR PDB; 1HBM; 16-AUG-01. DR PDB; 1HBN; 16-AUG-01. DR PDB; 1HBO; 16-AUG-01. DR PDB; 1HBU; 16-AUG-01. DR InterPro; IPR008924; MCR_alpha_beta_C. DR InterPro; IPR003179; MCR_beta. DR InterPro; IPR009024; MCR_fer_like. DR Pfam; PF02241; MCR_beta; 1. DR Pfam; PF02783; MCR_beta_N; 1. DR PIRSF; PIRSF000263; Meth_CoM_rd_beta; 1. KW Methanogenesis; Transferase; Multigene family; 3D-structure. FT INIT_MET 0 0 FT STRAND 6 10 FT TURN 12 13 FT STRAND 16 22 FT HELIX 23 26 FT TURN 28 30 FT HELIX 32 43 FT STRAND 44 48 FT HELIX 49 58 FT TURN 59 59 FT TURN 64 65 FT TURN 69 70 FT TURN 77 77 FT HELIX 78 80 FT HELIX 81 92 FT TURN 96 97 FT STRAND 101 105 FT HELIX 106 108 FT TURN 109 109 FT STRAND 110 114 FT HELIX 117 121 FT TURN 122 122 FT TURN 127 127 FT HELIX 128 145 FT TURN 146 146 FT TURN 149 151 FT HELIX 152 160 FT TURN 161 165 FT TURN 170 171 FT STRAND 174 175 FT HELIX 181 183 FT TURN 187 188 FT HELIX 190 192 FT HELIX 196 202 FT TURN 203 205 FT HELIX 207 224 FT TURN 225 228 FT HELIX 230 232 FT HELIX 233 244 FT HELIX 247 249 FT HELIX 250 258 FT TURN 259 261 FT HELIX 264 277 FT TURN 278 279 FT STRAND 282 287 FT TURN 288 289 FT STRAND 290 294 FT HELIX 298 320 FT TURN 321 321 FT HELIX 323 325 FT HELIX 326 341 FT HELIX 346 349 FT HELIX 350 360 FT TURN 361 362 FT HELIX 371 373 FT TURN 376 377 FT TURN 379 381 FT HELIX 389 398 FT HELIX 407 410 FT HELIX 412 418 FT TURN 419 420 FT HELIX 422 425 FT HELIX 427 438 FT TURN 439 442 SQ SEQUENCE 442 AA; 47108 MW; 9F7F032CBA07CD23 CRC64; AKFEDKVDLY DDRGNLVEEQ VPLEALSPLR NPAIKSIVQG IKRTVAVNLE GIENALKTAK VGGPACKIMG RELDLDIVGN AESIAAAAKE MIQVTEDDDT NVELLGGGKR ALVQVPSARF DVAAEYSAAP LVTATAFVQA IINEFDVSMY DANMVKAAVL GRYPQSVEYM GANIATMLDI PQKLEGPGYA LRNIMVNHVV AATLKNTLQA AALSTILEQT AMFEMGDAVG AFERMHLLGL AYQGMNADNL VFDLVKANGK EGTVGSVIAD LVERALEDGV IKVEKELTDY KVYGTDDLAM WNAYAAAGLM AATMVNQGAA RAAQGVSSTL LYYNDLIEFE TGLPSVDFGK VEGTAVGFSF FSHSIYGGGG PGIFNGNHIV TRHSKGFAIP CVAAAMALDA GTQMFSPEAT SGLIKEVFSQ VDEFREPLKY VVEAAAEIKN EI //