ID CHMU_YEAST Reviewed; 256 AA. AC P32178; D6W465; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 02-SEP-2026, entry version 199. DE RecName: Full=Chorismate mutase {ECO:0000303|PubMed:2187528}; DE Short=CM {ECO:0000303|PubMed:10428795}; DE EC=5.4.99.5 {ECO:0000269|PubMed:10428795, ECO:0000269|PubMed:10894726, ECO:0000269|PubMed:2187528, ECO:0000269|PubMed:2646272, ECO:0000269|PubMed:31498992, ECO:0000269|PubMed:9642265}; GN Name=ARO7 {ECO:0000303|PubMed:2187528, ECO:0000312|SGD:S000006264}; GN Synonyms=OSM2; OrderedLocusNames=YPR060C; ORFNames=YP9499.15C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY RP REGULATION, INDUCTION, AND MUTAGENESIS OF THR-226. RC STRAIN=ATCC 26109 / X2180; RX PubMed=2646272; DOI=10.1128/jb.171.3.1245-1253.1989; RA Schmidheini T., Sperisen P., Paravicini G., Huetter R., Braus G.H.; RT "A single point mutation results in a constitutively activated and RT feedback-resistant chorismate mutase of Saccharomyces cerevisiae."; RL J. Bacteriol. 171:1245-1253(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169875; DOI=10.1038/387s103; RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., RA Vo D.H., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."; RL Nature 387:103-105(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP PROTEIN SEQUENCE OF 30-33; 119-124; 133-137; 163-168 AND 191-204, FUNCTION, RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, RP PATHWAY, SUBUNIT, AND MUTAGENESIS OF THR-226. RX PubMed=2187528; DOI=10.1021/bi00467a011; RA Schmidheini T., Moesch H.U., Evans J.N., Braus G.; RT "Yeast allosteric chorismate mutase is locked in the activated state by a RT single amino acid substitution."; RL Biochemistry 29:3660-3668(1990). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL RP PROPERTIES, TYROSINE AND TRYPTOPHAN BINDING, AND MUTAGENESIS OF ARG-75; RP ARG-76; GLY-141; SER-142 AND THR-145. RX PubMed=9642265; DOI=10.1074/jbc.273.27.17012; RA Schnappauf G., Krappmann S., Braus G.H.; RT "Tyrosine and tryptophan act through the same binding site at the dimer RT interface of yeast chorismate mutase."; RL J. Biol. Chem. 273:17012-17017(1998). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF RP THR-226. RC STRAIN=ATCC 26786 / X2180-1A {ECO:0000303|PubMed:10428795}; RX PubMed=10428795; DOI=10.1074/jbc.274.32.22275; RA Krappmann S., Helmstaedt K., Gerstberger T., Eckert S., Hoffmann B., RA Hoppert M., Schnappauf G., Braus G.H.; RT "The aroC gene of Aspergillus nidulans codes for a monofunctional, RT allosterically regulated chorismate mutase."; RL J. Biol. Chem. 274:22275-22282(1999). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=ATCC 26786 / X2180-1A {ECO:0000303|PubMed:10894726}; RX PubMed=10894726; DOI=10.1128/jb.182.15.4188-4197.2000; RA Krappmann S., Pries R., Gellissen G., Hiller M., Braus G.H.; RT "HARO7 encodes chorismate mutase of the methylotrophic yeast Hansenula RT polymorpha and is derepressed upon methanol utilization."; RL J. Bacteriol. 182:4188-4197(2000). RN [9] RP SUBCELLULAR LOCATION. RC STRAIN=ATCC 200060 / W303 {ECO:0000303|PubMed:12455686}; RX PubMed=12455686; DOI=10.1128/ec.1.5.663-672.2002; RA Pries R., Boemeke K., Irniger S., Grundmann O., Braus G.H.; RT "Amino acid-dependent Gcn4p stability regulation occurs exclusively in the RT yeast nucleus."; RL Eukaryot. Cell 1:663-672(2002). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=31498992; DOI=10.1021/acs.biochem.9b00721; RA Gorman S.D., Boehr D.D.; RT "Energy and Enzyme Activity Landscapes of Yeast Chorismate Mutase at RT Cellular Concentrations of Allosteric Effectors."; RL Biochemistry 58:4058-4069(2019). RN [12] {ECO:0007744|PDB:1CSM} RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH TRYPTOPHAN. RX PubMed=7971967; DOI=10.1073/pnas.91.23.10814; RA Xue Y., Lipscomb W.N., Graf R., Schnappauf G., Braus G.; RT "The crystal structure of allosteric chorismate mutase at 2.2-A RT resolution."; RL Proc. Natl. Acad. Sci. U.S.A. 91:10814-10818(1994). RN [13] {ECO:0007744|PDB:2CSM} RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH TYROSINE. RX PubMed=8622937; DOI=10.1073/pnas.93.8.3330; RA Straeter N., Haakansson K., Schnappauf G., Braus G., Lipscomb W.N.; RT "Crystal structure of the T state of allosteric yeast chorismate mutase and RT comparison with the R state."; RL Proc. Natl. Acad. Sci. U.S.A. 93:3330-3334(1996). RN [14] {ECO:0007744|PDB:3CSM, ECO:0007744|PDB:4CSM, ECO:0007744|PDB:5CSM} RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)IN COMPLEXES WITH TRYPTOPHAN; TYROSINE RP AND INHIBITOR. RX PubMed=9384560; DOI=10.1016/s0969-2126(97)00294-3; RA Straeter N., Schnappauf G., Braus G., Lipscomb W.N.; RT "Mechanisms of catalysis and allosteric regulation of yeast chorismate RT mutase from crystal structures."; RL Structure 5:1437-1452(1997). CC -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to CC prephenate (PubMed:10428795, PubMed:10894726, PubMed:2187528, CC PubMed:2646272, PubMed:31498992, PubMed:9642265). Acts at the first CC branch point in the aromatic amino acid pathway where it steers CC biosynthesis towards phenylalanine and tyrosine, and away from CC tryptophan (Probable). {ECO:0000269|PubMed:10428795, CC ECO:0000269|PubMed:10894726, ECO:0000269|PubMed:2187528, CC ECO:0000269|PubMed:2646272, ECO:0000269|PubMed:31498992, CC ECO:0000269|PubMed:9642265, ECO:0000305|PubMed:2187528}. CC -!- CATALYTIC ACTIVITY: CC Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; CC Evidence={ECO:0000269|PubMed:10428795, ECO:0000269|PubMed:10894726, CC ECO:0000269|PubMed:2187528, ECO:0000269|PubMed:2646272, CC ECO:0000269|PubMed:31498992, ECO:0000269|PubMed:9642265}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13898; CC Evidence={ECO:0000269|PubMed:10428795, ECO:0000269|PubMed:10894726, CC ECO:0000269|PubMed:2187528, ECO:0000269|PubMed:2646272, CC ECO:0000269|PubMed:31498992, ECO:0000269|PubMed:9642265}; CC -!- ACTIVITY REGULATION: Each dimer has two allosteric binding sites that CC can bind the regulatory effectors tryptophan or tyrosine CC (PubMed:10428795, PubMed:2187528, PubMed:31498992, PubMed:9642265). Can CC bind either one tryptophan or one tyrosine, two tryptophan or two CC tyrosine or one tryptophan and one tyrosine, which differentially CC affect the catalytic activity (PubMed:31498992). Activated by CC tryptophan and subject to feedback inhibition by tyrosine CC (PubMed:10428795, PubMed:2187528, PubMed:2646272, PubMed:31498992). In CC the presence of both tryptophan and tyrosine, the enzyme is in the CC activated state (PubMed:2646272, PubMed:31498992). CC {ECO:0000269|PubMed:10428795, ECO:0000269|PubMed:2187528, CC ECO:0000269|PubMed:2646272, ECO:0000269|PubMed:31498992, CC ECO:0000269|PubMed:9642265}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=3.8 mM for chorismate (at 30 degrees Celsius) CC {ECO:0000269|PubMed:2187528, ECO:0000269|PubMed:9642265}; CC KM=0.4 mM for chorismate (in the presence of 10 uM of tryptophan and CC at 30 degrees Celsius) {ECO:0000269|PubMed:9642265}; CC KM=0.4 mM for chorismate (in the presence of 100 uM of phenylalanine CC and at 30 degrees Celsius) {ECO:0000269|PubMed:9642265}; CC Note=kcat is 176 sec(-1) for chorismate (PubMed:2187528). kcat is 176 CC sec(-1) for chorismate (in the presence of 10 uM of tryptophan) CC (PubMed:2187528). kcat is 348 sec(-1) for chorismate (in the presence CC of 10 uM of tryptophan and at 30 degrees Celsius) (PubMed:9642265). CC kcat is 129 sec(-1) for chorismate (in the presence of 300 uM of CC tyrosine) (PubMed:2187528). kcat is 387 sec(-1) for chorismate (in CC the presence of 100 uM of tyrosine and at 30 degrees Celsius) CC (PubMed:9642265). kcat is 320 sec(-1) for chorismate (in the presence CC of 100 uM of phenylalanine and at 30 degrees Celsius) CC (PubMed:9642265). {ECO:0000269|PubMed:2187528, CC ECO:0000269|PubMed:9642265}; CC pH dependence: CC Optimum pH isin the absence of effectors. Optimum pH is 7 in the CC presence of tryptophan. Optimum pH is 5 in the presence of tyrosine. CC {ECO:0000269|PubMed:2187528}; CC Temperature dependence: CC Optimum temperature is <38 degrees Celsius. CC {ECO:0000269|PubMed:10894726}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis; CC prephenate from chorismate: step 1/1. {ECO:0000305|PubMed:2187528}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:2187528}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12455686}. CC -!- INDUCTION: Not affected by altering tryptophan or tyrosine levels. CC {ECO:0000269|PubMed:2646272}. 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; M24517; AAB59309.1; -; Genomic_DNA. DR EMBL; Z49219; CAA89177.1; -; Genomic_DNA. DR EMBL; Z71255; CAA95004.1; -; Genomic_DNA. DR EMBL; AY693179; AAT93198.1; -; Genomic_DNA. DR EMBL; BK006949; DAA11481.1; -; Genomic_DNA. DR PIR; A45921; A45921. DR RefSeq; NP_015385.1; NM_001184157.1. DR PDB; 1CSM; X-ray; 2.20 A; A/B=1-256. DR PDB; 2CSM; X-ray; 2.80 A; A=1-256. DR PDB; 3CSM; X-ray; 3.00 A; A/B=1-256. DR PDB; 4CSM; X-ray; 2.80 A; A/B=1-256. DR PDB; 5CSM; X-ray; 2.00 A; A=1-256. DR AlphaFoldDB; P32178; -. DR MDRepo; P32178; -. DR SMR; P32178; -. DR BioGRID; 36233; 269. DR FunCoup; P32178; 237. DR IntAct; P32178; 3. DR STRING; 4932.YPR060C; -. DR iPTMnet; P32178; -. DR PaxDb; 4932-YPR060C; -. DR PeptideAtlas; P32178; -. DR EnsemblFungi; YPR060C_mRNA; YPR060C; YPR060C. DR GeneID; 856173; -. DR KEGG; sce:YPR060C; -. DR AGR; SGD:S000006264; -. DR SGD; S000006264; ARO7. DR VEuPathDB; FungiDB:YPR060C; -. DR eggNOG; KOG0795; Eukaryota. DR HOGENOM; CLU_057757_0_0_1; -. DR InParanoid; P32178; -. DR OMA; FLDWALM; -. DR OrthoDB; 191918at2759; -. DR BioCyc; YEAST:YPR060C-MONOMER; -. DR BRENDA; 5.4.99.5; 984. DR UniPathway; UPA00120; UER00203. DR BioGRID-ORCS; 856173; 1 hit in 10 CRISPR screens. DR EvolutionaryTrace; P32178; -. DR PRO; PR:P32178; -. DR Proteomes; UP000002311; Chromosome XVI. DR RNAct; P32178; protein. DR GO; GO:0005737; C:cytoplasm; EXP:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0004106; F:chorismate mutase activity; IDA:UniProtKB. DR GO; GO:0072545; F:L-tyrosine binding; IDA:UniProtKB. DR GO; GO:0120284; F:tryptophan binding; IDA:UniProtKB. DR GO; GO:0046417; P:chorismate metabolic process; IDA:UniProtKB. DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IMP:SGD. DR GO; GO:0006571; P:L-tyrosine biosynthetic process; IMP:SGD. DR FunFam; 1.10.590.10:FF:000002; Chorismate mutase; 1. DR Gene3D; 1.10.590.10; Chorismate mutase, AroQ class superfamily, eukaryotic; 1. DR InterPro; IPR036263; Chorismate_II_sf. DR InterPro; IPR008238; Chorismate_mutase_AroQ_euk. DR InterPro; IPR037039; CM_AroQ_sf_eucaryotic. DR InterPro; IPR002701; CM_II_prokaryot. DR NCBIfam; TIGR01802; CM_pl-yst; 1. DR PANTHER; PTHR21145; CHORISMATE MUTASE; 1. DR PANTHER; PTHR21145:SF12; CHORISMATE MUTASE; 1. DR Pfam; PF01817; CM_2; 1. DR PIRSF; PIRSF017318; Chor_mut_AroQ_eu; 1. DR SUPFAM; SSF48600; Chorismate mutase II; 1. DR PROSITE; PS51169; CHORISMATE_MUT_3; 1. DR PDBsum; 1CSM; -. DR PDBsum; 2CSM; -. DR PDBsum; 3CSM; -. DR PDBsum; 4CSM; -. DR PDBsum; 5CSM; -. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; Amino-acid biosynthesis; KW Aromatic amino acid biosynthesis; Cytoplasm; Direct protein sequencing; KW Isomerase; Phenylalanine biosynthesis; Reference proteome; KW Tyrosine biosynthesis. FT CHAIN 1..256 FT /note="Chorismate mutase" FT /id="PRO_0000119204" FT DOMAIN 3..255 FT /note="Chorismate mutase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00516" FT BINDING 75 FT /ligand="L-tyrosine" FT /ligand_id="ChEBI:CHEBI:58315" FT /ligand_note="allosteric effector" FT /evidence="ECO:0000269|PubMed:8622937, FT ECO:0007744|PDB:2CSM" FT BINDING 76 FT /ligand="L-tyrosine" FT /ligand_id="ChEBI:CHEBI:58315" FT /ligand_note="allosteric effector" FT /evidence="ECO:0000269|PubMed:8622937, FT ECO:0007744|PDB:2CSM" FT BINDING 138 FT /ligand="L-tryptophan" FT /ligand_id="ChEBI:CHEBI:57912" FT /ligand_note="allosteric effector" FT /evidence="ECO:0000269|PubMed:7971967, FT ECO:0007744|PDB:1CSM" FT BINDING 139 FT /ligand="L-tryptophan" FT /ligand_id="ChEBI:CHEBI:57912" FT /ligand_note="allosteric effector" FT /evidence="ECO:0000269|PubMed:7971967, FT ECO:0007744|PDB:1CSM" FT BINDING 139 FT /ligand="L-tyrosine" FT /ligand_id="ChEBI:CHEBI:58315" FT /ligand_note="allosteric effector" FT /evidence="ECO:0000269|PubMed:8622937, FT ECO:0007744|PDB:2CSM" FT BINDING 141 FT /ligand="L-tryptophan" FT /ligand_id="ChEBI:CHEBI:57912" FT /ligand_note="allosteric effector" FT /evidence="ECO:0000269|PubMed:7971967, FT ECO:0007744|PDB:1CSM" FT BINDING 141 FT /ligand="L-tyrosine" FT /ligand_id="ChEBI:CHEBI:58315" FT /ligand_note="allosteric effector" FT /evidence="ECO:0000269|PubMed:8622937, FT ECO:0007744|PDB:2CSM" FT BINDING 142 FT /ligand="L-tryptophan" FT /ligand_id="ChEBI:CHEBI:57912" FT /ligand_note="allosteric effector" FT /evidence="ECO:0000269|PubMed:7971967, FT ECO:0007744|PDB:1CSM" FT BINDING 142 FT /ligand="L-tyrosine" FT /ligand_id="ChEBI:CHEBI:58315" FT /ligand_note="allosteric effector" FT /evidence="ECO:0000269|PubMed:8622937, FT ECO:0007744|PDB:2CSM" FT BINDING 145 FT /ligand="L-tyrosine" FT /ligand_id="ChEBI:CHEBI:58315" FT /ligand_note="allosteric effector" FT /evidence="ECO:0000269|PubMed:8622937, FT ECO:0007744|PDB:2CSM" FT MUTAGEN 75 FT /note="R->A: Severely decreases tyrosine and tryptophan FT binding, resulting in loss of enzyme activity regulation by FT effectors." FT /evidence="ECO:0000269|PubMed:9642265" FT MUTAGEN 76 FT /note="R->A: Severely decreases tyrosine and tryptophan FT binding, resulting in loss of enzyme activity regulation by FT effectors." FT /evidence="ECO:0000269|PubMed:9642265" FT MUTAGEN 141 FT /note="G->S: Abolishes tyrosine and tryptophan binding, FT resulting in loss of enzyme activity regulation by FT effectors." FT /evidence="ECO:0000269|PubMed:9642265" FT MUTAGEN 142 FT /note="S->A: Decreases tyrosine and tryptophan binding, FT resulting in attenuated enzyme activity regulation by FT effectors." FT /evidence="ECO:0000269|PubMed:9642265" FT MUTAGEN 145 FT /note="T->V: Decreases tyrosine binding, resulting in loss FT of enzyme inhibition by tyrosine. Enhances activation by FT phenylalanine." FT /evidence="ECO:0000269|PubMed:9642265" FT MUTAGEN 226 FT /note="T->D: Constitutively inactive. Unresponsive to FT tryptophan activation." FT /evidence="ECO:0000269|PubMed:10428795" FT MUTAGEN 226 FT /note="T->I: Constitutively active. Unresponsive to FT tryptophan activation and tyrosine feedback inhibition." FT /evidence="ECO:0000269|PubMed:10428795, FT ECO:0000269|PubMed:2187528, ECO:0000269|PubMed:2646272" FT HELIX 6..9 FT /evidence="ECO:0007829|PDB:5CSM" FT HELIX 12..34 FT /evidence="ECO:0007829|PDB:5CSM" FT HELIX 40..42 FT /evidence="ECO:0007829|PDB:5CSM" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:1CSM" FT HELIX 59..73 FT /evidence="ECO:0007829|PDB:5CSM" FT HELIX 76..78 FT /evidence="ECO:0007829|PDB:5CSM" FT TURN 87..89 FT /evidence="ECO:0007829|PDB:5CSM" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:5CSM" FT HELIX 100..102 FT /evidence="ECO:0007829|PDB:5CSM" FT HELIX 108..110 FT /evidence="ECO:0007829|PDB:5CSM" FT HELIX 114..120 FT /evidence="ECO:0007829|PDB:5CSM" FT HELIX 121..125 FT /evidence="ECO:0007829|PDB:5CSM" FT HELIX 126..129 FT /evidence="ECO:0007829|PDB:5CSM" FT STRAND 130..134 FT /evidence="ECO:0007829|PDB:5CSM" FT HELIX 137..139 FT /evidence="ECO:0007829|PDB:2CSM" FT HELIX 140..159 FT /evidence="ECO:0007829|PDB:5CSM" FT HELIX 161..170 FT /evidence="ECO:0007829|PDB:5CSM" FT HELIX 173..181 FT /evidence="ECO:0007829|PDB:5CSM" FT HELIX 185..191 FT /evidence="ECO:0007829|PDB:5CSM" FT HELIX 195..211 FT /evidence="ECO:0007829|PDB:5CSM" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:1CSM" FT HELIX 227..233 FT /evidence="ECO:0007829|PDB:5CSM" FT HELIX 234..238 FT /evidence="ECO:0007829|PDB:5CSM" FT HELIX 239..251 FT /evidence="ECO:0007829|PDB:5CSM" FT TURN 252..254 FT /evidence="ECO:0007829|PDB:1CSM" SQ SEQUENCE 256 AA; 29747 MW; 8C6BEBEAA3497E23 CRC64; MDFTKPETVL NLQNIRDELV RMEDSIIFKF IERSHFATCP SVYEANHPGL EIPNFKGSFL DWALSNLEIA HSRIRRFESP DETPFFPDKI QKSFLPSINY PQILAPYAPE VNYNDKIKKV YIEKIIPLIS KRDGDDKNNF GSVATRDIEC LQSLSRRIHF GKFVAEAKFQ SDIPLYTKLI KSKDVEGIMK NITNSAVEEK ILERLTKKAE VYGVDPTNES GERRITPEYL VKIYKEIVIP ITKEVEVEYL LRRLEE //