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 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
//