ID TRES_MYCS2 Reviewed; 593 AA.
AC A0R6E0; I7GGI2;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=Trehalose synthase/amylase TreS {ECO:0000303|PubMed:18505459};
DE EC=3.2.1.1 {ECO:0000269|PubMed:18505459};
DE EC=5.4.99.16 {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994};
DE AltName: Full=Maltose alpha-D-glucosyltransferase {ECO:0000303|PubMed:18505459};
DE Short=MTase {ECO:0000303|PubMed:18505459};
GN Name=treS {ECO:0000303|PubMed:18505459};
GN OrderedLocusNames=MSMEG_6515, MSMEI_6343;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP ACTIVITY REGULATION.
RX PubMed=3294776; DOI=10.7164/antibiotics.40.563;
RA Kameda Y., Asano N., Yamaguchi T., Matsui K.;
RT "Validoxylamines as trehalase inhibitors.";
RL J. Antibiot. 40:563-565(1987).
RN [5]
RP FUNCTION AS A TREHALOSE SYNTHASE, CATALYTIC ACTIVITY, SUBUNIT, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 14468 / DSM 43277 / NCIB 9953 / NCTC 10265 / W-113, and
RC ATCC 700084 / mc(2)155;
RX PubMed=15511231; DOI=10.1111/j.1432-1033.2004.04365.x;
RA Pan Y.T., Koroth Edavana V., Jourdian W.J., Edmondson R., Carroll J.D.,
RA Pastuszak I., Elbein A.D.;
RT "Trehalose synthase of Mycobacterium smegmatis: purification, cloning,
RT expression, and properties of the enzyme.";
RL Eur. J. Biochem. 271:4259-4269(2004).
RN [6]
RP FUNCTION AS A TREHALOSE SYNTHASE AND AMYLASE, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=18505459; DOI=10.1111/j.1742-4658.2008.06491.x;
RA Pan Y.T., Carroll J.D., Asano N., Pastuszak I., Edavana V.K., Elbein A.D.;
RT "Trehalose synthase converts glycogen to trehalose.";
RL FEBS J. 275:3408-3420(2008).
RN [7]
RP FUNCTION, ROLE IN CONVERSION OF TREHALOSE TO GLYCOGEN, DISRUPTION
RP PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 14468 / DSM 43277 / NCIB 9953 / NCTC 10265 / W-113;
RX PubMed=20118231; DOI=10.1074/jbc.m109.033944;
RA Elbein A.D., Pastuszak I., Tackett A.J., Wilson T., Pan Y.T.;
RT "Last step in the conversion of trehalose to glycogen: a mycobacterial
RT enzyme that transfers maltose from maltose 1-phosphate to glycogen.";
RL J. Biol. Chem. 285:9803-9812(2010).
RN [8]
RP FUNCTION, KINETIC PARAMETERS, CATALYTIC MECHANISM, ACTIVE SITE, AND
RP CATALYTIC ACTIVITY.
RX PubMed=21840994; DOI=10.1074/jbc.m111.280362;
RA Zhang R., Pan Y.T., He S., Lam M., Brayer G.D., Elbein A.D., Withers S.G.;
RT "Mechanistic analysis of trehalose synthase from mycobacterium smegmatis.";
RL J. Biol. Chem. 286:35601-35609(2011).
RN [9] {ECO:0007744|PDB:3ZO9, ECO:0007744|PDB:3ZOA}
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) IN COMPLEX WITH CALCIUM.
RX PubMed=23735230; DOI=10.1093/glycob/cwt044;
RA Caner S., Nguyen N., Aguda A., Zhang R., Pan Y.T., Withers S.G.,
RA Brayer G.D.;
RT "The structure of the Mycobacterium smegmatis trehalose synthase reveals an
RT unusual active site configuration and acarbose-binding mode.";
RL Glycobiology 23:1075-1083(2013).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=27513637; DOI=10.1371/journal.ppat.1005768;
RA Koliwer-Brandl H., Syson K., van de Weerd R., Chandra G., Appelmelk B.,
RA Alber M., Ioerger T.R., Jacobs W.R. Jr., Geurtsen J., Bornemann S.,
RA Kalscheuer R.;
RT "Metabolic network for the biosynthesis of intra- and extracellular alpha-
RT glucans required for virulence of Mycobacterium tuberculosis.";
RL PLoS Pathog. 12:E1005768-E1005768(2016).
CC -!- FUNCTION: Catalyzes the reversible interconversion of maltose and
CC trehalose by transglucosylation (PubMed:15511231, PubMed:18505459,
CC PubMed:20118231, PubMed:21840994). Maltose is the preferred substrate
CC (PubMed:15511231, PubMed:18505459). To a lesser extent, also displays
CC amylase activity, catalyzing the endohydrolysis of (1->4)-alpha-D-
CC glucosidic linkages in glycogen and maltooligosaccharides such as
CC maltoheptaose, to produce maltose which then can be converted to
CC trehalose (PubMed:18505459). TreS plays a key role in the utilization
CC of trehalose for the production of glycogen and alpha-glucan via the
CC TreS-Pep2 branch involved in the biosynthesis of maltose-1-phosphate
CC (M1P) (PubMed:20118231, PubMed:27513637). Might also function as a
CC sensor and/or regulator of trehalose levels within the cell. Thus, when
CC trehalose levels in the cell become dangerously low, TreS can expedite
CC the conversion of glycogen to maltose via its amylase activity and then
CC convert the maltose to trehalose; but this enzyme also can expedite or
CC promote the conversion of trehalose to glycogen when cytoplasmic
CC trehalose levels become too high. Is also able to catalyze the
CC hydrolytic cleavage of alpha-aryl glucosides, as well as alpha-glucosyl
CC fluoride in vitro. {ECO:0000269|PubMed:15511231,
CC ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:20118231,
CC ECO:0000269|PubMed:21840994, ECO:0000269|PubMed:27513637}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-maltose = alpha,alpha-trehalose; Xref=Rhea:RHEA:15145,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:17306; EC=5.4.99.16;
CC Evidence={ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459,
CC ECO:0000269|PubMed:21840994};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:18505459};
CC -!- ACTIVITY REGULATION: The amylase activity is stimulated by addition of
CC Ca(2+), but this cation and other divalent cations inhibit the
CC trehalose synthase activity. In addition, trehalose synthase activity,
CC but not amylase activity, is strongly inhibited, and in a competitive
CC manner, by validoxylamine. On the other hand, amylase, but not
CC trehalose synthase activity, is inhibited by the known transition-state
CC amylase inhibitor, acarbose, suggesting the possibility of two
CC different active sites. Other metal ions such as Mg(2+), Mn(2+), and
CC Co(2+) are also somewhat effective in the stimulation of amylase
CC activity, but Hg(2+), Cu(2+), Ni(2+) and Zn(2+) are inhibitory.
CC {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459,
CC ECO:0000269|PubMed:3294776}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.0 mM for maltose (at pH 6.8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459,
CC ECO:0000269|PubMed:21840994};
CC KM=87 mM for trehalose (at pH 6.8 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459,
CC ECO:0000269|PubMed:21840994};
CC KM=2.9 mM for 2,4-dinitrophenyl alpha-D-glucoside (at pH 6.8 and 37
CC degrees Celsius) {ECO:0000269|PubMed:15511231,
CC ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994};
CC KM=2.5 mM for 3,4-dinitrophenyl alpha-D-glucoside (at pH 6.8 and 37
CC degrees Celsius) {ECO:0000269|PubMed:15511231,
CC ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994};
CC KM=2.2 mM for 4-chloro-2-nitrophenyl alpha-D-glucoside (at pH 6.8 and
CC 37 degrees Celsius) {ECO:0000269|PubMed:15511231,
CC ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994};
CC KM=5.8 mM for 4-nitrophenyl alpha-D-glucoside (at pH 6.8 and 37
CC degrees Celsius) {ECO:0000269|PubMed:15511231,
CC ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994};
CC KM=0.7 mM for 2-nitrophenyl alpha-D-glucoside (at pH 6.8 and 37
CC degrees Celsius) {ECO:0000269|PubMed:15511231,
CC ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994};
CC KM=0.15 mM for alpha-glucosyl fluoride (at pH 6.8 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459,
CC ECO:0000269|PubMed:21840994};
CC pH dependence:
CC Optimum pH is between 6.0-6.2 for the amylase activity and 7.0 for
CC the trehalose synthase activity. {ECO:0000269|PubMed:15511231,
CC ECO:0000269|PubMed:18505459};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000269|PubMed:20118231, ECO:0000269|PubMed:27513637}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:15511231}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not accumulate
CC increased amounts of glycogen in the presence of trehalose and show
CC only a small effect in alpha-glucan (PubMed:20118231, PubMed:27513637).
CC Combined inactivation of treS with glgB or glgC completely blocks
CC alpha-glucan production (PubMed:27513637).
CC {ECO:0000269|PubMed:20118231, ECO:0000269|PubMed:27513637}.
CC -!- MISCELLANEOUS: Maltose-1-phosphate (M1P), the building block required
CC for alpha-glucan production, is generated by two alternative routes:
CC the TreS-Pep2 branch and the GlgC-GlgM branch, however it seems that
CC the GlgC-GlgM branch provides most of M1P for the GlgE pathway in
CC M.smegmatis. {ECO:0000269|PubMed:27513637}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. TreS
CC subfamily. {ECO:0000305}.
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DR EMBL; CP000480; ABK71531.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42769.1; -; Genomic_DNA.
DR RefSeq; WP_003897929.1; NZ_SIJM01000033.1.
DR RefSeq; YP_890728.1; NC_008596.1.
DR PDB; 3ZO9; X-ray; 1.84 A; A/B=1-593.
DR PDB; 3ZOA; X-ray; 1.85 A; A/B=1-593.
DR PDB; 5JY7; X-ray; 3.60 A; A/B/C/D/E/F/G/H=1-593.
DR PDBsum; 3ZO9; -.
DR PDBsum; 3ZOA; -.
DR PDBsum; 5JY7; -.
DR AlphaFoldDB; A0R6E0; -.
DR SMR; A0R6E0; -.
DR STRING; 246196.MSMEG_6515; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; 246196-MSMEI_6343; -.
DR GeneID; 66737787; -.
DR KEGG; msg:MSMEI_6343; -.
DR KEGG; msm:MSMEG_6515; -.
DR PATRIC; fig|246196.19.peg.6339; -.
DR eggNOG; COG0366; Bacteria.
DR OrthoDB; 9043248at2; -.
DR BioCyc; MetaCyc:MONOMER-6023; -.
DR BRENDA; 5.4.99.16; 3512.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0004556; F:alpha-amylase activity; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0047471; F:maltose alpha-D-glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0005977; P:glycogen metabolic process; IDA:UniProtKB.
DR GO; GO:0000023; P:maltose metabolic process; IDA:UniProtKB.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0005991; P:trehalose metabolic process; IDA:UniProtKB.
DR CDD; cd11334; AmyAc_TreS; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR032091; Malt_amylase_C.
DR InterPro; IPR045857; O16G_dom_2.
DR InterPro; IPR012810; TreS/a-amylase_N.
DR NCBIfam; TIGR02456; treS_nterm; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF219; MALTOSE ALPHA-D-GLUCOSYLTRANSFERASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF16657; Malt_amylase_C; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Glycogen biosynthesis;
KW Glycogen metabolism; Glycosidase; Hydrolase; Isomerase; Metal-binding;
KW Polysaccharide degradation; Reference proteome.
FT CHAIN 1..593
FT /note="Trehalose synthase/amylase TreS"
FT /id="PRO_0000412905"
FT ACT_SITE 230
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:21840994"
FT ACT_SITE 272
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:23735230,
FT ECO:0007744|PDB:3ZO9, ECO:0007744|PDB:3ZOA"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:23735230,
FT ECO:0007744|PDB:3ZO9, ECO:0007744|PDB:3ZOA"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:23735230,
FT ECO:0007744|PDB:3ZO9, ECO:0007744|PDB:3ZOA"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:23735230,
FT ECO:0007744|PDB:3ZO9, ECO:0007744|PDB:3ZOA"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:23735230,
FT ECO:0007744|PDB:3ZO9, ECO:0007744|PDB:3ZOA"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:3ZO9"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 139..146
FT /evidence="ECO:0007829|PDB:3ZO9"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:3ZO9"
FT TURN 171..175
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:3ZO9"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 206..222
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 247..263
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 302..312
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 316..323
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:3ZO9"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:3ZO9"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:3ZO9"
FT TURN 356..360
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 365..369
FT /evidence="ECO:0007829|PDB:3ZO9"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:3ZO9"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 385..397
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 398..405
FT /evidence="ECO:0007829|PDB:3ZO9"
FT TURN 406..411
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 434..437
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:3ZO9"
FT TURN 454..456
FT /evidence="ECO:0007829|PDB:3ZO9"
FT TURN 458..460
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 463..467
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 473..485
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 488..492
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 505..512
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 524..531
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 533..535
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:3ZO9"
FT HELIX 544..546
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 550..553
FT /evidence="ECO:0007829|PDB:3ZO9"
FT TURN 554..556
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 568..572
FT /evidence="ECO:0007829|PDB:3ZO9"
FT STRAND 577..583
FT /evidence="ECO:0007829|PDB:3ZO9"
SQ SEQUENCE 593 AA; 68201 MW; D63935658A86B6E4 CRC64;
MEEHTQGSHV EAGIVEHPNA EDFGHARTLP TDTNWFKHAV FYEVLVRAFY DSNADGIGDL
RGLTEKLDYI KWLGVDCLWL PPFYDSPLRD GGYDIRDFYK VLPEFGTVDD FVTLLDAAHR
RGIRIITDLV MNHTSDQHEW FQESRHNPDG PYGDFYVWSD TSDRYPDARI IFVDTEESNW
TFDPVRRQFY WHRFFSHQPD LNYDNPAVQE AMLDVLRFWL DLGIDGFRLD AVPYLFEREG
TNCENLPETH AFLKRCRKAI DDEYPGRVLL AEANQWPADV VAYFGDPDTG GDECHMAFHF
PLMPRIFMAV RRESRFPISE ILAQTPPIPD TAQWGIFLRN HDELTLEMVT DEERDYMYAE
YAKDPRMKAN VGIRRRLAPL LENDRNQIEL FTALLLSLPG SPVLYYGDEI GMGDIIWLGD
RDSVRTPMQW TPDRNAGFSK ATPGRLYLPP NQDAVYGYHS VNVEAQLDSS SSLLNWTRNM
LAVRSRHDAF AVGTFRELGG SNPSVLAYIR EVTRQQGDGG AKTDAVLCVN NLSRFPQPIE
LNLQQWAGYI PVEMTGYVEF PSIGQLPYLL TLPGHGFYWF QLREPDPEPG AQQ
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