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 10-APR-2019, entry version 125. 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 RT from 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., RA Seedorf H., 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 RT Methanobacterium thermoautotrophicum strain Marburg and delta H."; RL Eur. J. Biochem. 194:871-877(1990). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, RP ACTIVITY REGULATION, PATHWAY, AND SUBUNIT. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=3350018; RA Ellermann J., Hedderich R., Boecher R., Thauer R.K.; RT "The final step in methane formation. Investigations with highly RT purified 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; RA Goubeaud M., Schreiner G., Thauer R.K.; RT "Purified methyl-coenzyme-M reductase is activated when the enzyme- RT bound coenzyme F430 is reduced to the nickel(I) oxidation state by RT titanium(III) 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:0000244|PDB:1MRO} RP X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) OF 2-443 IN COMPLEX WITH RP COENZYME F430; COENZYME B; COENZYME M AND MCR SUBUNITS ALPHA AND RP GAMMA, 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 [9] {ECO:0000244|PDB:1HBM, ECO:0000244|PDB:1HBN, ECO:0000244|PDB:1HBO, ECO:0000244|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 RP ALPHA 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., 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). RN [10] {ECO:0000244|PDB:3M1V, ECO:0000244|PDB:3M2R, ECO:0000244|PDB:3M2U, ECO:0000244|PDB:3M2V, ECO:0000244|PDB:3M30, ECO:0000244|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 RP AND 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:0000244|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 RT reductase from Methanothermobacter marburgensis."; RL J. Am. Chem. Soc. 133:5626-5628(2011). RN [12] {ECO:0000244|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 RT Catalyzing Methane Formation."; RL Angew. Chem. Int. Ed. Engl. 55:10630-10633(2016). RN [13] {ECO:0000244|PDB:5G0R} RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH COENZYME B; RP COENZYME F430 AND MCR SUBUNITS ALPHA AND GAMMA, AND ACTIVITY RP 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., RA Yanez-Ruiz D.R., Duval S., Rumbeli R., Stemmler R.T., Thauer R.K., RA Kindermann M.; RT "Mode of action uncovered for the specific reduction of methane RT emissions 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 CC that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S- CC CH3 or 2-(methylthio)ethanesulfonate) using coenzyme B (CoB or 7- CC mercaptoheptanoylthreonine phosphate) as reductant which results CC in the production of methane and the mixed heterodisulfide of CoB CC and CoM (CoM-S-S-CoB). This is the final step in methanogenesis CC (PubMed:2269306, PubMed:3350018). 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:3350018}. CC -!- CATALYTIC ACTIVITY: CC Reaction=coenzyme B + methyl-coenzyme M = coenzyme M-coenzyme B CC heterodisulfide + methane; Xref=Rhea:RHEA:12532, CC ChEBI:CHEBI:16183, ChEBI:CHEBI:58286, ChEBI:CHEBI:58411, CC ChEBI:CHEBI:58596; EC=2.8.4.1; CC Evidence={ECO:0000269|PubMed:2269306, CC ECO:0000269|PubMed:25691570, ECO:0000269|PubMed:27140643, CC ECO:0000269|PubMed:3350018}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12533; CC Evidence={ECO:0000269|PubMed:27140643, CC ECO:0000305|PubMed:3350018}; CC -!- COFACTOR: CC Name=coenzyme F430; Xref=ChEBI:CHEBI:60540; CC Evidence={ECO:0000269|PubMed:3350018, CC ECO:0000269|PubMed:9030728, ECO:0000269|PubMed:9367957}; CC Note=Binds 2 coenzyme F430 non-covalently per MCR complex. CC Coenzyme F430 is a yellow nickel porphinoid (PubMed:3350018, CC PubMed:9367957). Methyl-coenzyme-M reductase is activated when the CC enzyme-bound coenzyme F430 is reduced to the Ni(I) oxidation state CC (PubMed:9030728). {ECO:0000269|PubMed:3350018, CC ECO:0000269|PubMed:9030728, ECO:0000269|PubMed:9367957}; CC -!- ACTIVITY REGULATION: Methyl-coenzyme M reductase activity is CC inhibited by 3-nitrooxypropanol (3-NOP) in vitro and in vivo, by CC oxidation of its active site Ni(I), which stops both growth and CC methanogenesis (PubMed:27140643). Is also inhibited by the CC reaction product CoM-S-S-CoB (PubMed:3350018). CC {ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:3350018}. CC -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; CC methane from methyl-coenzyme M: step 1/1. CC {ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:3350018}. CC -!- SUBUNIT: MCR is a hexamer of two alpha, two beta, and two gamma CC chains, forming a dimer of heterotrimers. CC {ECO:0000269|PubMed:2269306, ECO:0000269|PubMed:3350018, CC 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 CC cytoplasmic membrane, which implies "facultative" membrane CC association of the enzyme. {ECO:0000269|PubMed:23533332}. 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 contain mostly MCR I. {ECO:0000269|PubMed:2269306}. CC -!- MISCELLANEOUS: The MCR reaction has been shown to follow an CC ordered bi-bi ternary complex mechanism, in which methyl-SCoM must CC enter the MCR active site prior to CoB for a productive catalysis. CC {ECO:0000269|PubMed:25691570}. CC -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase beta CC subunit 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 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 ProteinModelPortal; P11560; -. DR SMR; P11560; -. DR EnsemblBacteria; ADL59131; ADL59131; MTBMA_c15520. DR GeneID; 9705261; -. DR KEGG; mmg:MTBMA_c15520; -. DR PATRIC; fig|79929.8.peg.1505; -. DR eggNOG; arCOG04860; Archaea. DR eggNOG; COG4054; LUCA. DR HOGENOM; HOG000225842; -. DR KO; K00401; -. DR OMA; TAMFEMG; -. DR OrthoDB; 25508at2157; -. DR BioCyc; MMAR79929:G1GML-1527-MONOMER; -. DR BRENDA; 2.8.4.1; 7427. DR UniPathway; UPA00646; UER00699. DR EvolutionaryTrace; P11560; -. DR Proteomes; UP000000345; Chromosome. DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IDA:MENGO. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR Gene3D; 1.20.840.10; -; 1. DR Gene3D; 3.30.70.470; -; 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 Pfam; PF02241; MCR_beta; 1. DR Pfam; PF02783; MCR_beta_N; 1. DR PIRSF; PIRSF000263; Meth_CoM_rd_beta; 1. DR SUPFAM; SSF48081; SSF48081; 1. DR SUPFAM; SSF55088; SSF55088; 1. DR TIGRFAMs; TIGR03257; met_CoM_red_bet; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; KW Methanogenesis; Transferase. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2269306}. FT CHAIN 2 443 Methyl-coenzyme M reductase I subunit FT beta. FT /FTId=PRO_0000147468. FT BINDING 367 367 Coenzyme M. {ECO:0000244|PDB:1HBN, FT ECO:0000244|PDB:1MRO, FT ECO:0000244|PDB:3M1V, FT ECO:0000244|PDB:3POT, FT ECO:0000244|PDB:5A0Y, FT ECO:0000269|PubMed:11491299, FT ECO:0000269|PubMed:20707311, FT ECO:0000269|PubMed:21438550, FT ECO:0000269|PubMed:27467699, FT ECO:0000269|PubMed:9367957}. FT BINDING 369 369 Coenzyme B; via amide nitrogen. FT {ECO:0000244|PDB:1HBN, FT ECO:0000244|PDB:1MRO, FT ECO:0000244|PDB:3M1V, FT ECO:0000244|PDB:3POT, FT ECO:0000244|PDB:5A0Y, FT ECO:0000244|PDB:5G0R, FT ECO:0000269|PubMed:11491299, FT ECO:0000269|PubMed:20707311, FT ECO:0000269|PubMed:21438550, FT ECO:0000269|PubMed:27140643, FT ECO:0000269|PubMed:27467699, FT ECO:0000269|PubMed:9367957}. FT STRAND 7 11 {ECO:0000244|PDB:5A0Y}. FT STRAND 17 23 {ECO:0000244|PDB:5A0Y}. FT HELIX 24 27 {ECO:0000244|PDB:5A0Y}. FT TURN 29 31 {ECO:0000244|PDB:5A0Y}. FT HELIX 33 44 {ECO:0000244|PDB:5A0Y}. FT STRAND 45 49 {ECO:0000244|PDB:5A0Y}. FT HELIX 50 59 {ECO:0000244|PDB:5A0Y}. FT HELIX 79 81 {ECO:0000244|PDB:5A0Y}. FT HELIX 82 93 {ECO:0000244|PDB:5A0Y}. FT STRAND 102 106 {ECO:0000244|PDB:5A0Y}. FT HELIX 107 109 {ECO:0000244|PDB:5A0Y}. FT STRAND 111 115 {ECO:0000244|PDB:5A0Y}. FT HELIX 118 122 {ECO:0000244|PDB:5A0Y}. FT STRAND 124 127 {ECO:0000244|PDB:5A0Y}. FT HELIX 129 146 {ECO:0000244|PDB:5A0Y}. FT TURN 150 152 {ECO:0000244|PDB:5A0Y}. FT HELIX 153 161 {ECO:0000244|PDB:5A0Y}. FT TURN 162 166 {ECO:0000244|PDB:5A0Y}. FT STRAND 167 169 {ECO:0000244|PDB:5A0Y}. FT STRAND 174 176 {ECO:0000244|PDB:5A0Y}. FT HELIX 182 184 {ECO:0000244|PDB:5A0Y}. FT HELIX 191 193 {ECO:0000244|PDB:5A0Y}. FT HELIX 197 203 {ECO:0000244|PDB:5A0Y}. FT TURN 204 206 {ECO:0000244|PDB:5A0Y}. FT HELIX 208 225 {ECO:0000244|PDB:5A0Y}. FT TURN 226 229 {ECO:0000244|PDB:5A0Y}. FT HELIX 231 233 {ECO:0000244|PDB:5A0Y}. FT HELIX 234 245 {ECO:0000244|PDB:5A0Y}. FT HELIX 248 250 {ECO:0000244|PDB:5A0Y}. FT HELIX 251 259 {ECO:0000244|PDB:5A0Y}. FT TURN 260 262 {ECO:0000244|PDB:5A0Y}. FT HELIX 265 278 {ECO:0000244|PDB:5A0Y}. FT STRAND 283 288 {ECO:0000244|PDB:5A0Y}. FT STRAND 291 295 {ECO:0000244|PDB:5A0Y}. FT HELIX 299 321 {ECO:0000244|PDB:5A0Y}. FT HELIX 324 326 {ECO:0000244|PDB:5A0Y}. FT HELIX 327 342 {ECO:0000244|PDB:5A0Y}. FT HELIX 347 350 {ECO:0000244|PDB:5A0Y}. FT HELIX 351 361 {ECO:0000244|PDB:5A0Y}. FT STRAND 364 368 {ECO:0000244|PDB:5A0Y}. FT HELIX 372 374 {ECO:0000244|PDB:5A0Y}. FT TURN 380 382 {ECO:0000244|PDB:5A0Y}. FT STRAND 384 389 {ECO:0000244|PDB:5A0Y}. FT HELIX 390 398 {ECO:0000244|PDB:5A0Y}. FT HELIX 408 411 {ECO:0000244|PDB:5A0Y}. FT HELIX 413 419 {ECO:0000244|PDB:5A0Y}. FT HELIX 423 426 {ECO:0000244|PDB:5A0Y}. FT HELIX 428 439 {ECO:0000244|PDB:5A0Y}. FT HELIX 440 442 {ECO:0000244|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 //