P21110O27201Q50487MCRX_METTHMethyl-coenzyme M reductase II subunit alphaMCR II alpha2.8.4.1Coenzyme-B sulfoethylthiotransferase alphamrtAMTH_1129Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)Methanobacterium thermoautotrophicumArchaeaEuryarchaeotaMethanomada groupMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacterGrowth phase-dependent transcription of the genes that encode the two methyl coenzyme M reductase isoenzymes and N5-methyltetrahydromethanopterin:coenzyme M methyltransferase in Methanobacterium thermoautotrophicum delta H.NUCLEOTIDE SEQUENCE [GENOMIC DNA]Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]Two genetically distinct methyl-coenzyme M reductases in Methanobacterium thermoautotrophicum strain Marburg and delta H.PROTEIN SEQUENCE OF 1-15FUNCTIONCATALYTIC ACTIVITYSUBUNITComponent of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2-(methylthio)ethanesulfonate) using coenzyme B (CoB or 7-mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and CoM (CoM-S-S-CoB). This is the final step in methanogenesis.coenzyme B + methyl-coenzyme M = coenzyme M-coenzyme B heterodisulfide + methanecoenzyme F430Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme F430 is a yellow nickel porphinoid. Methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced to the Ni(I) oxidation state.One-carbon metabolism; methyl-coenzyme M reduction; methane from methyl-coenzyme M: step 1/1.MCR is a hexamer of two alpha, two beta, and two gamma chains, forming a dimer of heterotrimers.There are two MCR complexes in this bacteria. MCR II is expressed in the early growth phase. Late growth cells contain mostly MCR I.The alpha subunit contains six modified amino acids near the active site region. Is methylated on His-260, Arg-274, Gln-402 and Cys-454, probably by the action of specific S-adenosylmethionine-dependent methyltransferases. Also contains a thioglycine at position 447, forming a thiopeptide bond. Contains a didehydroaspartate residue at position 452 (By similarity). The methylation on C5 of Arg-274 is a post-translational methylation not essential in vivo, but which plays a role for the stability and structural integrity of MCR (By similarity).Belongs to the methyl-coenzyme M reductase alpha subunit family.Direct protein sequencingMetal-bindingMethanogenesisMethylationNickelReference proteomeTransferasecoenzyme F430Nicoenzyme Bligand shared between two alpha subunitscoenzyme Bligand shared between two alpha subunitscoenzyme Bligand shared between two alpha subunitscoenzyme Mcoenzyme MLHYIIVKKEQLKMDEKKLFLTALKKKFEVEDPDEKYTNFYCFGGWEQSARKKEFTEYAKKAAEKRGGIPFYNPDIGVPLGQRKLMAYRVSGTDAYVEGDDLHFVNNAAIQQMVDDIKRTVIVGMDTAHAVLEKRLGVEVTPETINEYMEAINHALPGGAVVQEHMVEVHPGLVEDCYAKIFTGDDNLADELDKRILIDINKEFPEEQAEQLKSYIGNRTYQVNRVPTIVVRTCDGGTVSRWSAMQIGMSFISAYKLCAGEAAIADFSYAAKHADVIEMGTIMPARRARGPNEPGGVAFGTFADIVQASRVSDDPAKISLEVIAGAAALYDQVWLGSYMSGGVGFTQYATAAYTDDILDDFVYYGMEYVDDKYGICGTKPTMDVVRDISTEVTLYSLEQYEEYPTLLEDHFGGSQRAAVAAAAAGCSTAFATGNSNAGINGWYLSQILHKEAHSRLGFYGYDLQDQCGASNSLSIRSDEGLIHELRGPNYPNYAMNVGHQPEYAGIAQAPHAARGDAFCTNPLIKVAFADKDLSFDFTSPRKSIAAGALREFMPEGERDLIIPAGK
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