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Database: UniProt/SWISS-PROT
Entry: TRES_MYCS2
LinkDB: TRES_MYCS2
Original site: TRES_MYCS2 
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-SEP-2017, entry version 77.
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   Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
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
RT   orthology and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   ENZYME REGULATION.
RX   PubMed=3294776;
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,
RP   SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME
RP   REGULATION, AND 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.,
RA   Carroll J.D., 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, ENZYME 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.,
RA   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.,
RA   Withers S.G.;
RT   "Mechanistic analysis of trehalose synthase from mycobacterium
RT   smegmatis.";
RL   J. Biol. Chem. 286:35601-35609(2011).
RN   [9] {ECO:0000244|PDB:3ZO9, ECO:0000244|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
RT   reveals an unusual active site configuration and acarbose-binding
RT   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.,
RA   Appelmelk B., Alber M., Ioerger T.R., Jacobs W.R. Jr., Geurtsen J.,
RA   Bornemann S., Kalscheuer R.;
RT   "Metabolic network for the biosynthesis of intra- and extracellular
RT   alpha-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
CC       substrate (PubMed:15511231, PubMed:18505459). To a lesser extent,
CC       also displays amylase activity, catalyzing the endohydrolysis of
CC       (1->4)-alpha-D-glucosidic linkages in glycogen and
CC       maltooligosaccharides such as maltoheptaose, to produce maltose
CC       which then can be converted to trehalose (PubMed:18505459). TreS
CC       plays a key role in the utilization of trehalose for the
CC       production of glycogen and alpha-glucan via the TreS-Pep2 branch
CC       involved in the biosynthesis of maltose-1-phosphate (M1P)
CC       (PubMed:20118231, PubMed:27513637). Might also function as a
CC       sensor and/or regulator of trehalose levels within the cell. Thus,
CC       when trehalose levels in the cell become dangerously low, TreS can
CC       expedite the conversion of glycogen to maltose via its amylase
CC       activity and then convert the maltose to trehalose; but this
CC       enzyme also can expedite or promote the conversion of trehalose to
CC       glycogen when cytoplasmic trehalose levels become too high. Is
CC       also able to catalyze the hydrolytic cleavage of alpha-aryl
CC       glucosides, as well as alpha-glucosyl fluoride in vitro.
CC       {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459,
CC       ECO:0000269|PubMed:20118231, ECO:0000269|PubMed:21840994,
CC       ECO:0000269|PubMed:27513637}.
CC   -!- CATALYTIC ACTIVITY: Maltose = alpha,alpha-trehalose.
CC       {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459,
CC       ECO:0000269|PubMed:21840994}.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-alpha-D-glucosidic
CC       linkages in polysaccharides containing three or more (1->4)-alpha-
CC       linked D-glucose units. {ECO:0000269|PubMed:18505459}.
CC   -!- ENZYME REGULATION: The amylase activity is stimulated by addition
CC       of Ca(2+), but this cation and other divalent cations inhibit the
CC       trehalose synthase activity. In addition, trehalose synthase
CC       activity, but not amylase activity, is strongly inhibited, and in
CC       a competitive manner, by validoxylamine. On the other hand,
CC       amylase, but not trehalose synthase activity, is inhibited by the
CC       known transition-state amylase inhibitor, acarbose, suggesting the
CC       possibility of two different active sites. Other metal ions such
CC       as Mg(2+), Mn(2+), and Co(2+) are also somewhat effective in the
CC       stimulation of amylase activity, but Hg(2+), Cu(2+), Ni(2+) and
CC       Zn(2+) are inhibitory. {ECO:0000269|PubMed:15511231,
CC       ECO:0000269|PubMed:18505459, 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
CC         37 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
CC         37 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
CC         6.8 and 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,
CC         ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994};
CC       pH dependence:
CC         Optimum pH is between 6.0-6.2 for the amylase activity and 7.0
CC         for the trehalose synthase activity.
CC         {ECO:0000269|PubMed:15511231, 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
CC       show only a small effect in alpha-glucan (PubMed:20118231,
CC       PubMed:27513637). Combined inactivation of treS with glgB or glgC
CC       completely blocks alpha-glucan production (PubMed:27513637).
CC       {ECO:0000269|PubMed:20118231, ECO:0000269|PubMed:27513637}.
CC   -!- MISCELLANEOUS: Maltose-1-phosphate (M1P), the building block
CC       required for alpha-glucan production, is generated by two
CC       alternative routes: the TreS-Pep2 branch and the GlgC-GlgM branch,
CC       however it seems that the GlgC-GlgM branch provides most of M1P
CC       for the GlgE pathway in M.smegmatis.
CC       {ECO:0000269|PubMed:27513637}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. TreS
CC       subfamily. {ECO:0000305}.
DR   EMBL; CP000480; ABK71531.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP42769.1; -; Genomic_DNA.
DR   RefSeq; WP_003897929.1; NZ_CP009494.1.
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   ProteinModelPortal; A0R6E0; -.
DR   SMR; A0R6E0; -.
DR   STRING; 246196.MSMEG_6515; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ABK71531; ABK71531; MSMEG_6515.
DR   EnsemblBacteria; AFP42769; AFP42769; MSMEI_6343.
DR   GeneID; 4533171; -.
DR   KEGG; msb:LJ00_32205; -.
DR   KEGG; msg:MSMEI_6343; -.
DR   KEGG; msm:MSMEG_6515; -.
DR   PATRIC; fig|246196.19.peg.6339; -.
DR   eggNOG; ENOG4105CG3; Bacteria.
DR   eggNOG; COG0366; LUCA.
DR   HOGENOM; HOG000220639; -.
DR   KO; K05343; -.
DR   OMA; VDVQKTQ; -.
DR   OrthoDB; POG091H07NZ; -.
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:0103025; F:alpha-amylase activity (releasing maltohexaose); IEA:UniProtKB-EC.
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   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR032091; Malt_amylase_C.
DR   InterPro; IPR012810; TreS/a-amylase_N.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16657; Malt_amylase_C; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   TIGRFAMs; TIGR02456; treS_nterm; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Carbohydrate metabolism; Complete proteome;
KW   Glycogen biosynthesis; Glycogen metabolism; Glycosidase; Hydrolase;
KW   Isomerase; Metal-binding; Polysaccharide degradation;
KW   Reference proteome.
FT   CHAIN         1    593       Trehalose synthase/amylase TreS.
FT                                /FTId=PRO_0000412905.
FT   ACT_SITE    230    230       Nucleophile.
FT                                {ECO:0000269|PubMed:21840994}.
FT   ACT_SITE    272    272       Proton donor.
FT                                {ECO:0000250|UniProtKB:Q9ZEU2}.
FT   METAL       132    132       Calcium. {ECO:0000244|PDB:3ZO9,
FT                                ECO:0000244|PDB:3ZOA,
FT                                ECO:0000269|PubMed:23735230}.
FT   METAL       200    200       Calcium. {ECO:0000244|PDB:3ZO9,
FT                                ECO:0000244|PDB:3ZOA,
FT                                ECO:0000269|PubMed:23735230}.
FT   METAL       234    234       Calcium; via carbonyl oxygen.
FT                                {ECO:0000244|PDB:3ZO9,
FT                                ECO:0000244|PDB:3ZOA,
FT                                ECO:0000269|PubMed:23735230}.
FT   METAL       235    235       Calcium; via carbonyl oxygen.
FT                                {ECO:0000244|PDB:3ZO9,
FT                                ECO:0000244|PDB:3ZOA,
FT                                ECO:0000269|PubMed:23735230}.
FT   METAL       237    237       Calcium. {ECO:0000244|PDB:3ZO9,
FT                                ECO:0000244|PDB:3ZOA,
FT                                ECO:0000269|PubMed:23735230}.
FT   BINDING      90     90       Substrate.
FT                                {ECO:0000250|UniProtKB:Q9ZEU2}.
FT   BINDING     133    133       Substrate.
FT                                {ECO:0000250|UniProtKB:Q9ZEU2}.
FT   BINDING     198    198       Substrate.
FT                                {ECO:0000250|UniProtKB:Q9ZEU2}.
FT   BINDING     228    228       Substrate.
FT                                {ECO:0000250|UniProtKB:Q9ZEU2}.
FT   BINDING     341    341       Substrate.
FT                                {ECO:0000250|UniProtKB:Q9ZEU2}.
FT   BINDING     342    342       Substrate.
FT                                {ECO:0000250|UniProtKB:Q9ZEU2}.
FT   HELIX        20     22       {ECO:0000244|PDB:3ZO9}.
FT   HELIX        35     38       {ECO:0000244|PDB:3ZO9}.
FT   STRAND       41     43       {ECO:0000244|PDB:3ZO9}.
FT   HELIX        46     49       {ECO:0000244|PDB:3ZO9}.
FT   STRAND       52     57       {ECO:0000244|PDB:3ZO9}.
FT   HELIX        60     65       {ECO:0000244|PDB:3ZO9}.
FT   HELIX        67     73       {ECO:0000244|PDB:3ZO9}.
FT   STRAND       77     80       {ECO:0000244|PDB:3ZO9}.
FT   TURN         89     92       {ECO:0000244|PDB:3ZO9}.
FT   STRAND       96    101       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       103    105       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       108    120       {ECO:0000244|PDB:3ZO9}.
FT   STRAND      124    130       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       139    146       {ECO:0000244|PDB:3ZO9}.
FT   TURN        151    154       {ECO:0000244|PDB:3ZO9}.
FT   STRAND      158    162       {ECO:0000244|PDB:3ZO9}.
FT   TURN        171    175       {ECO:0000244|PDB:3ZO9}.
FT   STRAND      179    182       {ECO:0000244|PDB:3ZO9}.
FT   TURN        184    186       {ECO:0000244|PDB:3ZO9}.
FT   STRAND      188    191       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       206    222       {ECO:0000244|PDB:3ZO9}.
FT   STRAND      226    231       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       232    234       {ECO:0000244|PDB:3ZO9}.
FT   STRAND      243    245       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       247    263       {ECO:0000244|PDB:3ZO9}.
FT   STRAND      268    272       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       277    280       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       281    284       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       287    289       {ECO:0000244|PDB:3ZO9}.
FT   STRAND      295    298       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       302    312       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       316    323       {ECO:0000244|PDB:3ZO9}.
FT   STRAND      333    336       {ECO:0000244|PDB:3ZO9}.
FT   TURN        343    345       {ECO:0000244|PDB:3ZO9}.
FT   TURN        352    354       {ECO:0000244|PDB:3ZO9}.
FT   TURN        356    360       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       361    363       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       365    369       {ECO:0000244|PDB:3ZO9}.
FT   TURN        370    372       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       377    380       {ECO:0000244|PDB:3ZO9}.
FT   TURN        381    383       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       385    397       {ECO:0000244|PDB:3ZO9}.
FT   STRAND      398    405       {ECO:0000244|PDB:3ZO9}.
FT   TURN        406    411       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       416    418       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       422    424       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       434    437       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       443    445       {ECO:0000244|PDB:3ZO9}.
FT   STRAND      446    448       {ECO:0000244|PDB:3ZO9}.
FT   TURN        454    456       {ECO:0000244|PDB:3ZO9}.
FT   TURN        458    460       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       463    467       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       473    485       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       488    492       {ECO:0000244|PDB:3ZO9}.
FT   STRAND      494    497       {ECO:0000244|PDB:3ZO9}.
FT   STRAND      505    512       {ECO:0000244|PDB:3ZO9}.
FT   STRAND      524    531       {ECO:0000244|PDB:3ZO9}.
FT   STRAND      533    535       {ECO:0000244|PDB:3ZO9}.
FT   STRAND      537    541       {ECO:0000244|PDB:3ZO9}.
FT   HELIX       544    546       {ECO:0000244|PDB:3ZO9}.
FT   STRAND      550    553       {ECO:0000244|PDB:3ZO9}.
FT   TURN        554    556       {ECO:0000244|PDB:3ZO9}.
FT   STRAND      568    572       {ECO:0000244|PDB:3ZO9}.
FT   STRAND      577    583       {ECO:0000244|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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