CHMU_YEAST
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 03-AUG-2022, entry version 184.
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;
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:2646272, PubMed:2187528, PubMed:10894726,
CC PubMed:31498992, PubMed:9642265, PubMed:10428795). 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:31498992, PubMed:2187528, PubMed:10428795, 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:31498992, PubMed:2646272, PubMed:2187528). 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}.
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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 PDBsum; 1CSM; -.
DR PDBsum; 2CSM; -.
DR PDBsum; 3CSM; -.
DR PDBsum; 4CSM; -.
DR PDBsum; 5CSM; -.
DR AlphaFoldDB; P32178; -.
DR SMR; P32178; -.
DR BioGRID; 36233; 262.
DR IntAct; P32178; 3.
DR STRING; 4932.YPR060C; -.
DR MaxQB; P32178; -.
DR PaxDb; P32178; -.
DR PRIDE; P32178; -.
DR EnsemblFungi; YPR060C_mRNA; YPR060C; YPR060C.
DR GeneID; 856173; -.
DR KEGG; sce:YPR060C; -.
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 BioCyc; YEAST:YPR060C-MON; -.
DR BRENDA; 5.4.99.5; 984.
DR UniPathway; UPA00120; UER00203.
DR EvolutionaryTrace; P32178; -.
DR PRO; PR:P32178; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P32178; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004106; F:chorismate mutase activity; IDA:UniProtKB.
DR GO; GO:0120284; F:tryptophan binding; IDA:UniProtKB.
DR GO; GO:0072545; F:tyrosine binding; IDA:UniProtKB.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central.
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:tyrosine biosynthetic process; IMP:SGD.
DR Gene3D; 1.10.590.10; -; 1.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR008238; Chorismate_mutase_AroQ_euk.
DR InterPro; IPR037039; CM_AroQ_sf_eucaryotic.
DR PANTHER; PTHR21145; PTHR21145; 1.
DR PIRSF; PIRSF017318; Chor_mut_AroQ_eu; 1.
DR SUPFAM; SSF48600; SSF48600; 1.
DR TIGRFAMs; TIGR01802; CM_pl-yst; 1.
DR PROSITE; PS51169; CHORISMATE_MUT_3; 1.
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 108..110
FT /evidence="ECO:0007829|PDB:5CSM"
FT HELIX 114..124
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..236
FT /evidence="ECO:0007829|PDB:5CSM"
FT HELIX 238..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
