ID MCRA_METTM Reviewed; 550 AA. AC P11558; D9PY29; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 154. DE RecName: Full=Methyl-coenzyme M reductase I subunit alpha {ECO:0000303|PubMed:2269306}; DE Short=MCR I alpha {ECO:0000303|PubMed:2269306}; DE EC=2.8.4.1 {ECO:0000269|PubMed:2269306, ECO:0000269|PubMed:25691570, ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:3350018}; DE AltName: Full=Coenzyme-B sulfoethylthiotransferase alpha; GN Name=mcrA; OrderedLocusNames=MTBMA_c15480; 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 from RT 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., Seedorf H., RA 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 2-19, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, SUBUNIT, AND DEVELOPMENTAL STAGE. 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 Methanobacterium RT thermoautotrophicum strain Marburg and delta H."; RL Eur. J. Biochem. 194:871-877(1990). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE RP SPECIFICITY, COFACTOR, ACTIVITY REGULATION, PATHWAY, AND SUBUNIT. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=3350018; DOI=10.1111/j.1432-1033.1988.tb13941.x; RA Ellermann J., Hedderich R., Boecher R., Thauer R.K.; RT "The final step in methane formation. Investigations with highly purified RT methyl-CoM reductase (component C) from Methanobacterium RT thermoautotrophicum (strain Marburg)."; RL Eur. J. Biochem. 172:669-677(1988). RN [5] RP COFACTOR. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=9030728; DOI=10.1111/j.1432-1033.1997.00110.x; RA Goubeaud M., Schreiner G., Thauer R.K.; RT "Purified methyl-coenzyme-M reductase is activated when the enzyme-bound RT coenzyme F430 is reduced to the nickel(I) oxidation state by titanium(III) RT citrate."; RL Eur. J. Biochem. 243:110-114(1997). RN [6] RP METHYLATION AT HIS-257; ARG-271; GLN-400 AND CYS-452, AND THIOCARBOXYLATION RP AT GLY-445. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=10660523; DOI=10.1074/jbc.275.6.3755; RA Selmer T., Kahnt J., Goubeaud M., Shima S., Grabarse W., Ermler U., RA Thauer R.K.; RT "The biosynthesis of methylated amino acids in the active site region of RT methyl-coenzyme M reductase."; RL J. Biol. Chem. 275:3755-3760(2000). RN [7] RP SUBCELLULAR LOCATION. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=23533332; DOI=10.1155/2013/920241; RA Wrede C., Walbaum U., Ducki A., Heieren I., Hoppert M.; RT "Localization of methyl-Coenzyme M reductase as metabolic marker for RT diverse methanogenic Archaea."; RL Archaea 2013:920241-920241(2013). RN [8] RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND REACTION MECHANISM. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=25691570; DOI=10.1074/jbc.m115.636761; RA Wongnate T., Ragsdale S.W.; RT "The reaction mechanism of methyl-coenzyme M reductase: how an enzyme RT enforces strict binding order."; RL J. Biol. Chem. 290:9322-9334(2015). RN [9] {ECO:0007744|PDB:1MRO} RP X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) OF 2-549 IN COMPLEX WITH COENZYME RP F430; COENZYME B; COENZYME M AND MCR SUBUNITS BETA AND GAMMA, METHYLATION RP AT HIS-257; ARG-271; GLN-400 AND CYS-452, THIOCARBOXYLATION AT GLY-445, RP COFACTOR, AND SUBUNIT. 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 [10] {ECO:0007744|PDB:1HBM, ECO:0007744|PDB:1HBN, ECO:0007744|PDB:1HBO, ECO:0007744|PDB:1HBU} RP X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) OF 2-550 IN COMPLEXES WITH RP COM-S-S-COB; COENZYME B; COENZYME F430; COENZYME M AND MCR SUBUNITS BETA RP AND GAMMA, METHYLATION AT HIS-257; ARG-271; GLN-400 AND CYS-452, AND RP THIOCARBOXYLATION AT GLY-445. 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., Thauer R.K., RA Lamzin V., Ermler U.; RT "On the mechanism of biological methane formation: structural evidence for RT conformational changes in methyl-coenzyme M reductase upon substrate RT binding."; RL J. Mol. Biol. 309:315-330(2001). RN [11] {ECO:0007744|PDB:3M1V, ECO:0007744|PDB:3M2R, ECO:0007744|PDB:3M2U, ECO:0007744|PDB:3M2V, ECO:0007744|PDB:3M30, ECO:0007744|PDB:3M32} RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 2-550 IN COMPLEXES WITH RP COM-S-S-COB; COENZYME B; COENZYME F430; COENZYME M; COENZYME B ANALOGS AND RP MCR SUBUNITS BETA AND GAMMA, METHYLATION AT HIS-257; ARG-271; GLN-400 AND RP CYS-452, AND THIOCARBOXYLATION AT GLY-445. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=20707311; DOI=10.1021/bi100458d; RA Cedervall P.E., Dey M., Pearson A.R., Ragsdale S.W., Wilmot C.M.; RT "Structural insight into methyl-coenzyme M reductase chemistry using RT coenzyme B analogues."; RL Biochemistry 49:7683-7693(2010). RN [12] {ECO:0007744|PDB:3POT} RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) IN COMPLEX WITH COENZYME F430; RP COENZYME B; COENZYME M AND MCR SUBUNITS BETA AND GAMMA, METHYLATION AT RP HIS-257; ARG-271; GLN-400 AND CYS-452, AND THIOCARBOXYLATION AT GLY-445. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=21438550; DOI=10.1021/ja110492p; RA Cedervall P.E., Dey M., Li X., Sarangi R., Hedman B., Ragsdale S.W., RA Wilmot C.M.; RT "Structural analysis of a Ni-methyl species in methyl-coenzyme M reductase RT from Methanothermobacter marburgensis."; RL J. Am. Chem. Soc. 133:5626-5628(2011). RN [13] {ECO:0007744|PDB:5A0Y} RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) IN COMPLEX WITH COENZYME F430; RP COENZYME B; COENZYME M AND MCR SUBUNITS BETA AND GAMMA, METHYLATION AT RP HIS-257; ARG-271; GLN-400 AND CYS-452, THIOCARBOXYLATION AT GLY-445, AND RP DEHYDROGENATION AT ASP-450. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=27467699; DOI=10.1002/anie.201603882; RA Wagner T., Kahnt J., Ermler U., Shima S.; RT "Didehydroaspartate Modification in Methyl-CoenzymeM Reductase Catalyzing RT Methane Formation."; RL Angew. Chem. Int. Ed. Engl. 55:10630-10633(2016). RN [14] {ECO:0007744|PDB:5G0R} RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH COENZYME B; COENZYME RP F430 AND MCR SUBUNITS BETA AND GAMMA, FUNCTION, CATALYTIC ACTIVITY, RP ACTIVITY REGULATION, AND PATHWAY. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=27140643; DOI=10.1073/pnas.1600298113; RA Duin E.C., Wagner T., Shima S., Prakash D., Cronin B., Yanez-Ruiz D.R., RA Duval S., Rumbeli R., Stemmler R.T., Thauer R.K., Kindermann M.; RT "Mode of action uncovered for the specific reduction of methane emissions RT from ruminants by the small molecule 3-nitrooxypropanol."; RL Proc. Natl. Acad. Sci. U.S.A. 113:6172-6177(2016). CC -!- FUNCTION: Component of the methyl-coenzyme M reductase (MCR) I that CC catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2- CC (methylthio)ethanesulfonate) using coenzyme B (CoB or 7- CC mercaptoheptanoylthreonine phosphate) as reductant which results in the CC production of methane and the mixed heterodisulfide of CoB and CoM CC (CoM-S-S-CoB). This is the final step in methanogenesis CC (PubMed:2269306, PubMed:3350018, PubMed:27140643). Neither N-6- CC mercaptohexanoylthreonine phosphate (H-S-HxoTP) nor N-8- CC mercaptooctanoylthreonine phosphate (H-SOcoTP) nor any other thiol CC compound such as CoA or CoM can substitute for CoB as the electron CC donor (PubMed:3350018). {ECO:0000269|PubMed:2269306, CC ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:3350018}. CC -!- CATALYTIC ACTIVITY: CC Reaction=coenzyme B + methyl-coenzyme M = coenzyme M-coenzyme B CC heterodisulfide + methane; Xref=Rhea:RHEA:12532, ChEBI:CHEBI:16183, CC ChEBI:CHEBI:58286, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=2.8.4.1; CC Evidence={ECO:0000269|PubMed:2269306, ECO:0000269|PubMed:25691570, CC ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:3350018}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12533; CC Evidence={ECO:0000269|PubMed:27140643, ECO:0000305|PubMed:3350018}; CC -!- COFACTOR: CC Name=coenzyme F430; Xref=ChEBI:CHEBI:60540; CC Evidence={ECO:0000269|PubMed:3350018, ECO:0000269|PubMed:9030728, CC ECO:0000269|PubMed:9367957}; CC Note=Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme CC F430 is a yellow nickel porphinoid (PubMed:3350018, PubMed:9367957). CC Methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme CC F430 is reduced to the Ni(I) oxidation state (PubMed:9030728). CC {ECO:0000269|PubMed:3350018, ECO:0000269|PubMed:9030728, CC ECO:0000269|PubMed:9367957}; CC -!- ACTIVITY REGULATION: Methyl-coenzyme M reductase activity is inhibited CC by 3-nitrooxypropanol (3-NOP) in vitro and in vivo, by oxidation of its CC active site Ni(I), which stops both growth and methanogenesis CC (PubMed:27140643). Is also inhibited by the reaction product CoM-S-S- CC CoB (PubMed:3350018). {ECO:0000269|PubMed:27140643, CC ECO:0000269|PubMed:3350018}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=75 uM for coenzyme B {ECO:0000269|PubMed:2269306, CC ECO:0000269|PubMed:3350018}; CC KM=4 mM for methyl-coenzyme M {ECO:0000269|PubMed:2269306, CC ECO:0000269|PubMed:3350018}; CC KM=169 uM for coenzyme B (at 25 degrees Celsius, under conditions in CC which the heterodisulfide product is recycled via reduction by CC hydroxocobalamin) {ECO:0000269|PubMed:25691570}; CC KM=42 uM for coenzyme B (at 25 degrees Celsius, under conditions in CC which the heterodisulfide product is not recycled) CC {ECO:0000269|PubMed:25691570}; CC Vmax=40 nmol/min/mg enzyme {ECO:0000269|PubMed:3350018}; CC Vmax=7.8 umol/min/mg enzyme (at 25 degrees Celsius, under conditions CC in which the heterodisulfide product is recycled via reduction by CC hydroxocobalamin) {ECO:0000269|PubMed:25691570}; CC Vmax=0.41 umol/min/mg enzyme (at 25 degrees Celsius, under conditions CC in which the heterodisulfide product is not recycled) CC {ECO:0000269|PubMed:25691570}; CC Note=kcat is 18 sec(-1) (at 25 degrees Celsius, under conditions in CC which the heterodisulfide product is recycled via reduction by CC hydroxocobalamin). kcat is 0.96 sec(-1) (at 25 degrees Celsius, under CC conditions in which the heterodisulfide product is not recycled). CC {ECO:0000269|PubMed:25691570}; CC -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; methane CC from methyl-coenzyme M: step 1/1. {ECO:0000269|PubMed:27140643, CC ECO:0000269|PubMed:3350018}. CC -!- SUBUNIT: MCR is a hexamer of two alpha, two beta, and two gamma chains, CC forming a dimer of heterotrimers. {ECO:0000269|PubMed:2269306, CC ECO:0000269|PubMed:3350018, ECO:0000269|PubMed:9367957}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23533332}. CC Note=Under growth limiting conditions on nickel-depleted media, a CC fraction of 70% of the enzyme is localized close to the cytoplasmic CC membrane, which implies 'facultative' membrane association of the CC enzyme. {ECO:0000269|PubMed:23533332}. CC -!- DEVELOPMENTAL STAGE: There are two MCR complexes in this bacteria. MCR CC II is expressed in the early growth phase. Late growth cells contain CC mostly MCR I. {ECO:0000269|PubMed:2269306}. CC -!- PTM: The alpha subunit contains six modified amino acids near the CC active site region (PubMed:27467699). Is methylated on His-257, Arg- CC 271, Gln-400 and Cys-452, probably by the action of specific S- CC adenosylmethionine-dependent methyltransferases. Also contains a CC thioglycine at position 445, forming a thiopeptide bond CC (PubMed:10660523, PubMed:9367957, PubMed:11491299, PubMed:20707311, CC PubMed:21438550, PubMed:27467699). Contains a didehydroaspartate CC residue at position 450 (PubMed:27467699). The methylation on C5 of CC Arg-271 is a post-translational methylation not essential in vivo, but CC which plays a role for the stability and structural integrity of MCR CC (By similarity). {ECO:0000250|UniProtKB:Q8THH1, CC ECO:0000269|PubMed:10660523, ECO:0000269|PubMed:11491299, CC ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550, CC ECO:0000269|PubMed:27467699, ECO:0000269|PubMed:9367957}. CC -!- MISCELLANEOUS: The MCR reaction has been shown to follow an ordered bi- CC bi ternary complex mechanism, in which methyl-SCoM must enter the MCR CC active site prior to CoB for a productive catalysis. CC {ECO:0000269|PubMed:25691570}. CC -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase alpha subunit CC family. {ECO:0000305}. 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; CAA30639.1; -; Genomic_DNA. DR EMBL; CP001710; ADL59127.1; -; Genomic_DNA. DR RefSeq; WP_013296337.1; NC_014408.1. DR PDB; 1HBM; X-ray; 1.80 A; A/D=2-550. DR PDB; 1HBN; X-ray; 1.16 A; A/D=2-550. DR PDB; 1HBO; X-ray; 1.78 A; A/D=2-550. DR PDB; 1HBU; X-ray; 1.90 A; A/D=2-550. DR PDB; 1MRO; X-ray; 1.16 A; A/D=2-549. DR PDB; 3M1V; X-ray; 1.45 A; A/D=2-550. DR PDB; 3M2R; X-ray; 1.30 A; A/D=2-550. DR PDB; 3M2U; X-ray; 1.40 A; A/D=2-550. DR PDB; 3M2V; X-ray; 1.80 A; A/D=2-550. DR PDB; 3M30; X-ray; 1.45 A; A/D=2-550. DR PDB; 3M32; X-ray; 1.35 A; A/D=2-550. DR PDB; 3POT; X-ray; 1.20 A; A/D=1-550. DR PDB; 5A0Y; X-ray; 1.10 A; A/D=1-550. DR PDB; 5G0R; X-ray; 1.25 A; A/D=1-550. DR PDB; 7B2H; X-ray; 2.12 A; A/D=1-550. DR PDB; 7SUC; X-ray; 1.90 A; A/a=2-549. DR PDB; 7SXM; X-ray; 2.50 A; A/D=2-549. 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 PDBsum; 7B2H; -. DR PDBsum; 7SUC; -. DR PDBsum; 7SXM; -. DR AlphaFoldDB; P11558; -. DR SMR; P11558; -. DR STRING; 79929.MTBMA_c15480; -. DR iPTMnet; P11558; -. DR PaxDb; 79929-MTBMA_c15480; -. DR GeneID; 9705257; -. DR KEGG; mmg:MTBMA_c15480; -. DR PATRIC; fig|79929.8.peg.1501; -. DR HOGENOM; CLU_493170_0_0_2; -. DR OrthoDB; 52468at2157; -. DR BRENDA; 2.8.4.1; 7427. DR UniPathway; UPA00646; UER00699. DR EvolutionaryTrace; P11558; -. DR Proteomes; UP000000345; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IDA:MENGO. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR Gene3D; 3.30.70.470; -; 1. DR Gene3D; 1.20.840.10; Methyl-coenzyme M reductase, alpha/beta subunit, C-terminal; 1. DR InterPro; IPR016212; Me_CoM_Rdtase_asu. DR InterPro; IPR008924; Me_CoM_Rdtase_asu/bsu_C. DR InterPro; IPR009047; Me_CoM_Rdtase_asu_C. DR InterPro; IPR003183; Me_CoM_Rdtase_asu_N. DR InterPro; IPR015811; Me_CoM_Rdtase_asu_N_sub1. DR InterPro; IPR015823; Me_CoM_Rdtase_asu_N_sub2. DR InterPro; IPR009024; Me_CoM_Rdtase_Fd-like_fold. DR NCBIfam; TIGR03256; met_CoM_red_alp; 1. DR Pfam; PF02249; MCR_alpha; 1. DR Pfam; PF02745; MCR_alpha_N; 1. DR PIRSF; PIRSF000262; MCR_alpha; 1. DR SUPFAM; SSF48081; Methyl-coenzyme M reductase alpha and beta chain C-terminal domain; 1. DR SUPFAM; SSF55088; Methyl-coenzyme M reductase subunits; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Metal-binding; KW Methanogenesis; Methylation; Nickel; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2269306" FT CHAIN 2..550 FT /note="Methyl-coenzyme M reductase I subunit alpha" FT /id="PRO_0000147456" FT BINDING 147 FT /ligand="coenzyme F430" FT /ligand_id="ChEBI:CHEBI:60540" FT /ligand_part="Ni" FT /ligand_part_id="ChEBI:CHEBI:28112" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:11491299, FT ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550, FT ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:27467699, FT ECO:0000269|PubMed:9367957, ECO:0007744|PDB:1HBN, FT ECO:0007744|PDB:1MRO, ECO:0007744|PDB:3M1V, FT ECO:0007744|PDB:3POT, ECO:0007744|PDB:5A0Y, FT ECO:0007744|PDB:5G0R" FT BINDING 225 FT /ligand="coenzyme B" FT /ligand_id="ChEBI:CHEBI:58596" FT /ligand_note="ligand shared between two alpha subunits" FT /note="in chain A" FT /evidence="ECO:0000269|PubMed:11491299, FT ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550, FT ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:27467699, FT ECO:0000269|PubMed:9367957, ECO:0007744|PDB:1HBN, FT ECO:0007744|PDB:1MRO, ECO:0007744|PDB:3M1V, FT ECO:0007744|PDB:3POT, ECO:0007744|PDB:5A0Y, FT ECO:0007744|PDB:5G0R" FT BINDING 256..257 FT /ligand="coenzyme B" FT /ligand_id="ChEBI:CHEBI:58596" FT /ligand_note="ligand shared between two alpha subunits" FT /note="in chain A" FT /evidence="ECO:0000269|PubMed:11491299, FT ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550, FT ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:27467699, FT ECO:0000269|PubMed:9367957, ECO:0007744|PDB:1HBN, FT ECO:0007744|PDB:1MRO, ECO:0007744|PDB:3M1V, FT ECO:0007744|PDB:3POT, ECO:0007744|PDB:5A0Y, FT ECO:0007744|PDB:5G0R" FT BINDING 270 FT /ligand="coenzyme B" FT /ligand_id="ChEBI:CHEBI:58596" FT /ligand_note="ligand shared between two alpha subunits" FT /note="in chain B" FT /evidence="ECO:0000269|PubMed:11491299, FT ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550, FT ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:27467699, FT ECO:0000269|PubMed:9367957, ECO:0007744|PDB:1HBN, FT ECO:0007744|PDB:1MRO, ECO:0007744|PDB:3M1V, FT ECO:0007744|PDB:3POT, ECO:0007744|PDB:5A0Y, FT ECO:0007744|PDB:5G0R" FT BINDING 333 FT /ligand="coenzyme M" FT /ligand_id="ChEBI:CHEBI:58319" FT /evidence="ECO:0000269|PubMed:11491299, FT ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550, FT ECO:0000269|PubMed:27467699, ECO:0000269|PubMed:9367957, FT ECO:0007744|PDB:1HBN, ECO:0007744|PDB:1MRO, FT ECO:0007744|PDB:3M1V, ECO:0007744|PDB:3POT, FT ECO:0007744|PDB:5A0Y" FT BINDING 444 FT /ligand="coenzyme M" FT /ligand_id="ChEBI:CHEBI:58319" FT /evidence="ECO:0000269|PubMed:11491299, FT ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550, FT ECO:0000269|PubMed:27467699, ECO:0000269|PubMed:9367957, FT ECO:0007744|PDB:1HBN, ECO:0007744|PDB:1MRO, FT ECO:0007744|PDB:3M1V, ECO:0007744|PDB:3POT, FT ECO:0007744|PDB:5A0Y" FT MOD_RES 257 FT /note="Pros-methylhistidine" FT /evidence="ECO:0000269|PubMed:10660523, FT ECO:0000269|PubMed:11491299, ECO:0000269|PubMed:20707311, FT ECO:0000269|PubMed:21438550, ECO:0000269|PubMed:27467699, FT ECO:0000269|PubMed:9367957" FT MOD_RES 271 FT /note="5-methylarginine" FT /evidence="ECO:0000269|PubMed:10660523, FT ECO:0000269|PubMed:11491299, ECO:0000269|PubMed:20707311, FT ECO:0000269|PubMed:21438550, ECO:0000269|PubMed:27467699, FT ECO:0000269|PubMed:9367957" FT MOD_RES 400 FT /note="2-methylglutamine" FT /evidence="ECO:0000269|PubMed:10660523, FT ECO:0000269|PubMed:11491299, ECO:0000269|PubMed:20707311, FT ECO:0000269|PubMed:21438550, ECO:0000269|PubMed:27467699, FT ECO:0000269|PubMed:9367957" FT MOD_RES 445 FT /note="1-thioglycine" FT /evidence="ECO:0000269|PubMed:10660523, FT ECO:0000269|PubMed:11491299, ECO:0000269|PubMed:20707311, FT ECO:0000269|PubMed:21438550, ECO:0000269|PubMed:27467699, FT ECO:0000269|PubMed:9367957" FT MOD_RES 450 FT /note="(Z)-2,3-didehydroaspartate" FT /evidence="ECO:0000269|PubMed:27467699" FT MOD_RES 452 FT /note="S-methylcysteine" FT /evidence="ECO:0000269|PubMed:10660523, FT ECO:0000269|PubMed:11491299, ECO:0000269|PubMed:20707311, FT ECO:0000269|PubMed:21438550, ECO:0000269|PubMed:27467699, FT ECO:0000269|PubMed:9367957" FT HELIX 7..13 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 30..33 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 35..51 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 60..62 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 71..74 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 83..86 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 88..90 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 92..102 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 104..109 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 110..118 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 126..139 FT /evidence="ECO:0007829|PDB:5A0Y" FT TURN 140..142 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 155..158 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 162..168 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 170..175 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 184..187 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 190..200 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 204..209 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 212..217 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 222..238 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 246..256 FT /evidence="ECO:0007829|PDB:5A0Y" FT TURN 257..259 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 269..271 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 275..277 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 278..280 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 283..289 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 292..294 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 300..316 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 317..323 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 331..335 FT /evidence="ECO:0007829|PDB:5A0Y" FT TURN 336..338 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 342..357 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 367..387 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 389..394 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 398..417 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 420..438 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 453..457 FT /evidence="ECO:0007829|PDB:5A0Y" FT TURN 462..464 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 468..470 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 476..478 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 482..484 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 485..499 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 507..512 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 518..520 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 525..533 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 544..546 FT /evidence="ECO:0007829|PDB:5A0Y" SQ SEQUENCE 550 AA; 60511 MW; D55A724B6CA9EFEE CRC64; MADKLFINAL KKKFEESPEE KKTTFYTLGG WKQSERKTEF VNAGKEVAAK RGIPQYNPDI GTPLGQRVLM PYQVSTTDTY VEGDDLHFVN NAAMQQMWDD IRRTVIVGLN HAHAVIEKRL GKEVTPETIT HYLETVNHAM PGAAVVQEHM VETHPALVAD SYVKVFTGND EIADEIDPAF VIDINKQFPE DQAETLKAEV GDGIWQVVRI PTIVSRTCDG ATTSRWSAMQ IGMSMISAYK QAAGEAATGD FAYAAKHAEV IHMGTYLPVR RARGENEPGG VPFGYLADIC QSSRVNYEDP VRVSLDVVAT GAMLYDQIWL GSYMSGGVGF TQYATAAYTD NILDDFTYFG KEYVEDKYGL CEAPNNMDTV LDVATEVTFY GLEQYEEYPA LLEDQFGGSQ RAAVVAAAAG CSTAFATGNA QTGLSGWYLS MYLHKEQHSR LGFYGYDLQD QCGASNVFSI RGDEGLPLEL RGPNYPNYAM NVGHQGEYAG ISQAPHAARG DAFVFNPLVK IAFADDNLVF DFTNVRGEFA KGALREFEPA GERALITPAK //