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 30-MAY-2000 (Rel. 39, Last annotation update) DE METHYL-COENZYME M REDUCTASE I BETA SUBUNIT (EC 1.8.-.-) (MCR I BETA). GN MCRB. OS Methanobacterium thermoautotrophicum (strain Marburg / DSM 2133). OC Archaea; Euryarchaeota; Methanobacteriales; Methanobacteriaceae; OC Methanobacterium. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 88115150. 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. 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. 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). CC -!- FUNCTION: THIS ENZYME COMPLEX CATALYZES THE FINAL STEP IN CC METHANOGENESIS, WHICH IS THE TERMINAL STEP OF ANAEROBIC CC DEGRADATION OF BIOMASS. CC -!- CATALYTIC ACTIVITY: REDUCTION OF METHYL-COENZYME M (2-(METHYLTHIO) CC ETHANESULFONIC ACID) WITH 7-MERCAPTOHEPTANOYLTHREONINE PHOSPHATE CC TO METHANE AND AN HETERODISULFIDE (CH(3)-S-COM + H-S-HTP = CH(4) + CC COM-S-S-HTP). CC -!- COFACTOR: THE ENZYME COMPLEX BINDS TIGHTLY (BUT NOT COVALENTLY) CC TO TWO MOLECULES OF COENZYME F430. F430 IS A YELLOW NICKEL CC PORPHINOID. 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 This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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. KW Methanogenesis; Oxidoreductase; Multigene family; 3D-structure. FT INIT_MET 0 0 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 //