MCRB_METTM
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 03-AUG-2022, entry version 137.
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}.
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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 PRIDE; P11560; -.
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; 25508at2157; -.
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; 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; 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
