ID MCRB_METTM Reviewed; 443 AA. AC P11560; D9PY33; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 08-NOV-2023, entry version 142. DE RecName: Full=Methyl-coenzyme M reductase I subunit beta {ECO:0000303|PubMed:2269306}; DE Short=MCR I beta {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 beta; GN Name=mcrB; OrderedLocusNames=MTBMA_c15520; 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 2-21, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND RP 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, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY RP 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 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 [7] RP CATALYTIC ACTIVITY, 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 [8] {ECO:0007744|PDB:1MRO} RP X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) OF 2-443 IN COMPLEX WITH COENZYME RP F430; COENZYME B; COENZYME M AND MCR SUBUNITS ALPHA AND GAMMA, COFACTOR, RP 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 [9] {ECO:0007744|PDB:1HBM, ECO:0007744|PDB:1HBN, ECO:0007744|PDB:1HBO, ECO:0007744|PDB:1HBU} RP X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) OF 2-443 IN COMPLEXES WITH RP COM-S-S-COB; COENZYME B; COENZYME F430; COENZYME M AND MCR SUBUNITS ALPHA RP AND GAMMA. 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 [10] {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 2-443 IN COMPLEXES WITH RP COM-S-S-COB; COENZYME B; COENZYME F430; COENZYME M; COENZYME B ANALOGS AND RP MCR SUBUNITS ALPHA AND GAMMA. 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 [11] {ECO:0007744|PDB:3POT} RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) IN COMPLEX WITH COENZYME F430; RP COENZYME B; COENZYME M AND MCR SUBUNITS ALPHA AND GAMMA. 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 [12] {ECO:0007744|PDB:5A0Y} RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) IN COMPLEX WITH COENZYME F430; RP COENZYME B; COENZYME M AND MCR SUBUNITS ALPHA AND GAMMA. 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 [13] {ECO:0007744|PDB:5G0R} RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH COENZYME B; COENZYME RP F430 AND MCR SUBUNITS ALPHA AND GAMMA, AND ACTIVITY REGULATION. 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). Neither N-6-mercaptohexanoylthreonine CC phosphate (H-S-HxoTP) nor N-8-mercaptooctanoylthreonine phosphate (H- CC SOcoTP) nor any other thiol compound such as CoA or CoM can substitute CC for CoB as the electron donor (PubMed:3350018). CC {ECO:0000269|PubMed:2269306, 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 -!- 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 -!- 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 beta 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; CAA30635.1; -; Genomic_DNA. DR EMBL; CP001710; ADL59131.1; -; Genomic_DNA. DR PIR; A28544; A28544. DR RefSeq; WP_013296341.1; NC_014408.1. DR PDB; 1HBM; X-ray; 1.80 A; B/E=2-443. DR PDB; 1HBN; X-ray; 1.16 A; B/E=2-443. DR PDB; 1HBO; X-ray; 1.78 A; B/E=2-443. DR PDB; 1HBU; X-ray; 1.90 A; B/E=2-443. DR PDB; 1MRO; X-ray; 1.16 A; B/E=2-443. DR PDB; 3M1V; X-ray; 1.45 A; B/E=2-443. DR PDB; 3M2R; X-ray; 1.30 A; B/E=2-443. DR PDB; 3M2U; X-ray; 1.40 A; B/E=2-443. DR PDB; 3M2V; X-ray; 1.80 A; B/E=2-443. DR PDB; 3M30; X-ray; 1.45 A; B/E=2-443. DR PDB; 3M32; X-ray; 1.35 A; B/E=2-443. DR PDB; 3POT; X-ray; 1.20 A; B/E=1-443. DR PDB; 5A0Y; X-ray; 1.10 A; B/E=1-443. DR PDB; 5G0R; X-ray; 1.25 A; B/E=1-443. DR PDB; 7B2H; X-ray; 2.12 A; B/E=1-443. DR PDB; 7SUC; X-ray; 1.90 A; B/b=2-443. DR PDB; 7SXM; X-ray; 2.50 A; B/E=2-443. 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; P11560; -. DR SMR; P11560; -. DR STRING; 79929.MTBMA_c15520; -. DR PaxDb; 79929-MTBMA_c15520; -. DR EnsemblBacteria; ADL59131; ADL59131; MTBMA_c15520. DR GeneID; 9705261; -. DR KEGG; mmg:MTBMA_c15520; -. DR PATRIC; fig|79929.8.peg.1505; -. DR HOGENOM; CLU_617682_0_0_2; -. DR OMA; TAMFEMG; -. DR OrthoDB; 52873at2157; -. DR BRENDA; 2.8.4.1; 25952. DR UniPathway; UPA00646; UER00699. DR EvolutionaryTrace; P11560; -. 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: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; IPR008924; Me_CoM_Rdtase_asu/bsu_C. DR InterPro; IPR015823; Me_CoM_Rdtase_asu_N_sub2. DR InterPro; IPR003179; Me_CoM_Rdtase_bsu. DR InterPro; IPR022679; Me_CoM_Rdtase_bsu_C. DR InterPro; IPR022680; Me_CoM_Rdtase_bsu_N. DR InterPro; IPR009024; Me_CoM_Rdtase_Fd-like_fold. DR NCBIfam; TIGR03257; met_CoM_red_bet; 1. DR Pfam; PF02241; MCR_beta; 1. DR Pfam; PF02783; MCR_beta_N; 1. DR PIRSF; PIRSF000263; Meth_CoM_rd_beta; 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; Methanogenesis; KW Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2269306" FT CHAIN 2..443 FT /note="Methyl-coenzyme M reductase I subunit beta" FT /id="PRO_0000147468" FT BINDING 367 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 369 FT /ligand="coenzyme B" FT /ligand_id="ChEBI:CHEBI:58596" 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 STRAND 7..11 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 13..15 FT /evidence="ECO:0007829|PDB:7B2H" FT STRAND 17..23 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 24..27 FT /evidence="ECO:0007829|PDB:5A0Y" FT TURN 29..31 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 33..44 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 45..49 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 50..59 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 79..81 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 82..93 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 102..106 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 107..109 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 111..115 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 118..122 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 124..127 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 129..146 FT /evidence="ECO:0007829|PDB:5A0Y" FT TURN 150..152 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 153..161 FT /evidence="ECO:0007829|PDB:5A0Y" FT TURN 162..166 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 167..169 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 182..184 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 191..193 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 197..203 FT /evidence="ECO:0007829|PDB:5A0Y" FT TURN 204..206 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 208..225 FT /evidence="ECO:0007829|PDB:5A0Y" FT TURN 226..229 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 231..233 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 234..245 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 248..250 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 251..259 FT /evidence="ECO:0007829|PDB:5A0Y" FT TURN 260..262 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 265..278 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 283..288 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 291..295 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 299..321 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 324..326 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 327..342 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 347..350 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 351..361 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 364..368 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 372..374 FT /evidence="ECO:0007829|PDB:5A0Y" FT TURN 380..382 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 384..389 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 390..398 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 408..411 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 413..419 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 423..426 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 428..439 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 440..442 FT /evidence="ECO:0007829|PDB:5A0Y" 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 //