AMY1_HORVU
ID AMY1_HORVU Reviewed; 438 AA.
AC P00693;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Alpha-amylase type A isozyme;
DE EC=3.2.1.1 {ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:18588886, ECO:0000269|PubMed:24089528, ECO:0000269|PubMed:7901200};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE AltName: Full=HvAMY1;
DE AltName: Full=Low pI alpha-amylase;
DE Flags: Precursor;
GN Name=AMY1.1;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Himalaya; TISSUE=Aleurone;
RX PubMed=6190808; DOI=10.1016/s0021-9258(20)82044-4;
RA Rogers J.C., Milliman C.;
RT "Isolation and sequence analysis of a barley alpha-amylase cDNA clone.";
RL J. Biol. Chem. 258:8169-8174(1983).
RN [2]
RP MUTAGENESIS OF HIS-117; ASP-204; GLU-229; TRP-303; HIS-314 AND ASP-315,
RP CATALYTIC ACTIVITY, AND ACTIVE SITE.
RX PubMed=7901200; DOI=10.1016/s0021-9258(18)41554-2;
RA Sogaard M., Kadziola A., Haser R., Svensson B.;
RT "Site-directed mutagenesis of histidine 93, aspartic acid 180, glutamic
RT acid 205, histidine 290, and aspartic acid 291 at the active site and
RT tryptophan 279 at the raw starch binding site in barley alpha-amylase 1.";
RL J. Biol. Chem. 268:22480-22484(1993).
RN [3]
RP MUTAGENESIS OF TRP-302; TRP-303 AND TYR-404.
RX PubMed=19606835; DOI=10.1021/bi900795a;
RA Nielsen M.M., Bozonnet S., Seo E.S., Motyan J.A., Andersen J.M.,
RA Dilokpimol A., Abou Hachem M., Gyemant G., Naested H., Kandra L.,
RA Sigurskjold B.W., Svensson B.;
RT "Two secondary carbohydrate binding sites on the surface of barley alpha-
RT amylase 1 have distinct functions and display synergy in hydrolysis of
RT starch granules.";
RL Biochemistry 48:7686-7697(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=24089528; DOI=10.1074/jbc.m113.514794;
RA Seung D., Thalmann M., Sparla F., Abou Hachem M., Lee S.K.,
RA Issakidis-Bourguet E., Svensson B., Zeeman S.C., Santelia D.;
RT "Arabidopsis thaliana AMY3 is a unique redox-regulated chloroplastic alpha-
RT amylase.";
RL J. Biol. Chem. 288:33620-33633(2013).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 25-428 IN COMPLEX WITH
RP CARBOHYDRATE AND CALCIUM IONS, AND COFACTOR.
RX PubMed=12906828; DOI=10.1016/s0969-2126(03)00151-5;
RA Robert X., Haser R., Gottschalk T.E., Ratajczak F., Driguez H.,
RA Svensson B., Aghajari N.;
RT "The structure of barley alpha-amylase isozyme 1 reveals a novel role of
RT domain C in substrate recognition and binding: a pair of sugar tongs.";
RL Structure 11:973-984(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 25-429 IN COMPLEXES WITH CALCIUM
RP IONS; ACARBOSE AND MALTOHEPTAOSE, CATALYTIC ACTIVITY, COFACTOR, AND
RP MUTAGENESIS OF ASP-204.
RX PubMed=16030022; DOI=10.1074/jbc.m505515200;
RA Robert X., Haser R., Mori H., Svensson B., Aghajari N.;
RT "Oligosaccharide binding to barley alpha-amylase 1.";
RL J. Biol. Chem. 280:32968-32978(2005).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 25-429 IN COMPLEX WITH CALCIUM
RP IONS AND ACARBOSE, COFACTOR, AND MUTAGENESIS OF TYR-404.
RX PubMed=17803687; DOI=10.1111/j.1742-4658.2007.06024.x;
RA Bozonnet S., Jensen M.T., Nielsen M.M., Aghajari N., Jensen M.H.,
RA Kramhoeft B., Willemoes M., Tranier S., Haser R., Svensson B.;
RT "The 'pair of sugar tongs' site on the non-catalytic domain C of barley
RT alpha-amylase participates in substrate binding and activity.";
RL FEBS J. 274:5055-5067(2007).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEXES WITH CALCIUM IONS AND
RP GLUCOSE, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF TYR-129; TYR-404
RP AND HIS-419.
RX PubMed=18588886; DOI=10.1016/j.febslet.2008.06.027;
RA Nielsen M.M., Seo E.S., Bozonnet S., Aghajari N., Robert X., Haser R.,
RA Svensson B.;
RT "Multi-site substrate binding and interplay in barley alpha-amylase 1.";
RL FEBS Lett. 582:2567-2571(2008).
CC -!- FUNCTION: Alpha-amylase displaying a robust amylolytic activity toward
CC p-nitrophenyl maltoheptaoside (BPNP-G7), amylopectin and beta-limit
CC dextrin (PubMed:24089528). {ECO:0000269|PubMed:24089528}.
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:16030022,
CC ECO:0000269|PubMed:18588886, ECO:0000269|PubMed:24089528,
CC ECO:0000269|PubMed:7901200};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:12906828, ECO:0000269|PubMed:16030022,
CC ECO:0000269|PubMed:17803687, ECO:0000269|PubMed:18588886};
CC Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000269|PubMed:12906828,
CC ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687,
CC ECO:0000269|PubMed:18588886};
CC -!- ACTIVITY REGULATION: Redox-insensitive. {ECO:0000269|PubMed:24089528}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5 with p-nitrophenyl maltoheptaoside or amylopectin
CC as substrate. {ECO:0000269|PubMed:24089528};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12906828,
CC ECO:0000269|PubMed:17803687}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- DEVELOPMENTAL STAGE: Production of alpha-amylase is hormonally
CC regulated. Germinating embryos produce the hormone gibberellic acid,
CC which within 10 hours stimulates the aleurone cells covering the
CC endosperm of the seed to produce alpha-amylase. The enzyme then
CC degrades the starch within the endosperm for use by the developing
CC plant embryo.
CC -!- MISCELLANEOUS: There are at least 4 types of alpha-amylase in barley.
CC -!- MISCELLANEOUS: Mutagenesis experiments indicate that His-117 and His-
CC 314 participate in transition state stabilization but not directly in
CC catalysis.
CC -!- MISCELLANEOUS: Binds starch not only at the active site, but also via
CC accessory binding sites on the protein surface that are important for
CC efficient binding to starch granules and thereby increase enzyme
CC activity.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; J01236; AAA32929.1; -; mRNA.
DR PIR; A00846; ALBH.
DR PDB; 1HT6; X-ray; 1.50 A; A=25-429.
DR PDB; 1P6W; X-ray; 2.00 A; A=25-429.
DR PDB; 1RP8; X-ray; 2.00 A; A=25-429.
DR PDB; 1RP9; X-ray; 2.00 A; A=25-429.
DR PDB; 1RPK; X-ray; 2.00 A; A=25-429.
DR PDB; 2QPS; X-ray; 2.20 A; A=25-429.
DR PDB; 2QPU; X-ray; 1.70 A; A/B/C=25-429.
DR PDB; 3BSG; X-ray; 1.95 A; A=25-438.
DR PDB; 3BSH; X-ray; 3.00 A; A=25-438.
DR PDBsum; 1HT6; -.
DR PDBsum; 1P6W; -.
DR PDBsum; 1RP8; -.
DR PDBsum; 1RP9; -.
DR PDBsum; 1RPK; -.
DR PDBsum; 2QPS; -.
DR PDBsum; 2QPU; -.
DR PDBsum; 3BSG; -.
DR PDBsum; 3BSH; -.
DR AlphaFoldDB; P00693; -.
DR SMR; P00693; -.
DR BindingDB; P00693; -.
DR ChEMBL; CHEMBL3616349; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR BRENDA; 3.2.1.1; 2687.
DR EvolutionaryTrace; P00693; -.
DR ExpressionAtlas; P00693; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005983; P:starch catabolic process; IEA:UniProt.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR012850; A-amylase_bs_C.
DR InterPro; IPR013775; A-amylase_pln.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF07821; Alpha-amyl_C2; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF001028; Alph-amls_plant; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00810; Alpha-amyl_C2; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Germination; Glycosidase;
KW Hydrolase; Metal-binding; Secreted; Signal.
FT SIGNAL 1..24
FT CHAIN 25..438
FT /note="Alpha-amylase type A isozyme"
FT /id="PRO_0000001404"
FT ACT_SITE 204
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:16030022,
FT ECO:0000305|PubMed:7901200"
FT ACT_SITE 229
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:7901200"
FT BINDING 69..71
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12906828"
FT BINDING 76..77
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:16030022"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12906828,
FT ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687,
FT ECO:0000269|PubMed:18588886"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12906828,
FT ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687,
FT ECO:0000269|PubMed:18588886"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12906828,
FT ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687,
FT ECO:0000269|PubMed:18588886"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12906828,
FT ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687,
FT ECO:0000269|PubMed:18588886"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12906828,
FT ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687,
FT ECO:0000269|PubMed:18588886"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12906828,
FT ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687,
FT ECO:0000269|PubMed:18588886"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12906828,
FT ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687,
FT ECO:0000269|PubMed:18588886"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12906828,
FT ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687,
FT ECO:0000269|PubMed:18588886"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12906828,
FT ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687,
FT ECO:0000269|PubMed:18588886"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12906828,
FT ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687,
FT ECO:0000269|PubMed:18588886"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12906828,
FT ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687,
FT ECO:0000269|PubMed:18588886"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12906828,
FT ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687,
FT ECO:0000269|PubMed:18588886"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12906828,
FT ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687,
FT ECO:0000269|PubMed:18588886"
FT BINDING 202..207
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12906828"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12906828,
FT ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687,
FT ECO:0000269|PubMed:18588886"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:16030022"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:16030022"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12906828,
FT ECO:0000305|PubMed:16030022"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:16030022,
FT ECO:0000305|PubMed:17803687"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:16030022"
FT BINDING 301..303
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12906828,
FT ECO:0000305|PubMed:16030022"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:16030022"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:16030022"
FT BINDING 399
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12906828,
FT ECO:0000305|PubMed:16030022"
FT BINDING 404..406
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12906828,
FT ECO:0000305|PubMed:16030022, ECO:0000305|PubMed:17803687,
FT ECO:0000305|PubMed:18588886"
FT BINDING 416..422
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12906828,
FT ECO:0000305|PubMed:16030022"
FT BINDING 426
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:16030022"
FT SITE 315
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:7901200"
FT MUTAGEN 117
FT /note="H->N: 20-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:7901200"
FT MUTAGEN 129
FT /note="Y->A: Reduces affinity for starch granules 3-fold."
FT /evidence="ECO:0000269|PubMed:18588886"
FT MUTAGEN 204
FT /note="D->A,N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16030022,
FT ECO:0000269|PubMed:7901200"
FT MUTAGEN 229
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7901200"
FT MUTAGEN 302
FT /note="W->A: Over 10-fold decrease in affinity for starch
FT granules. Abolishes binding of starch granules and reduces
FT activity towards starch granules by 99%; when associated
FT with A-303 and A-404."
FT /evidence="ECO:0000269|PubMed:19606835"
FT MUTAGEN 303
FT /note="W->A: Over 10-fold decrease in affinity for starch
FT granules. Abolishes binding of starch granules and reduces
FT activity towards starch granules by 99%; when associated
FT with A-302 and A-404."
FT /evidence="ECO:0000269|PubMed:19606835,
FT ECO:0000269|PubMed:7901200"
FT MUTAGEN 314
FT /note="H->N: 10-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:7901200"
FT MUTAGEN 315
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7901200"
FT MUTAGEN 404
FT /note="Y->A: Reduces affinity for starch granules 9-fold
FT and reduces activity by 90%. Abolishes binding of starch
FT granules and reduces activity towards starch granules by
FT 99%; when associated with A-302 and A-303."
FT /evidence="ECO:0000269|PubMed:17803687,
FT ECO:0000269|PubMed:18588886, ECO:0000269|PubMed:19606835"
FT MUTAGEN 404
FT /note="Y->M: Abolishes binding to cyclodextrin-Sepharose
FT and strongly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:17803687,
FT ECO:0000269|PubMed:18588886, ECO:0000269|PubMed:19606835"
FT MUTAGEN 419
FT /note="H->A: Slightly decreased catalytic activity."
FT /evidence="ECO:0000269|PubMed:18588886"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1HT6"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1HT6"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:1HT6"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:1HT6"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1HT6"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1HT6"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1HT6"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1HT6"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:1HT6"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:1HT6"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1HT6"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1HT6"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1HT6"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1HT6"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:1HT6"
FT HELIX 179..194
FT /evidence="ECO:0007829|PDB:1HT6"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:1HT6"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:1HT6"
FT HELIX 211..221
FT /evidence="ECO:0007829|PDB:1HT6"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1HT6"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1HT6"
FT HELIX 247..260
FT /evidence="ECO:0007829|PDB:1HT6"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:1HT6"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:1HT6"
FT HELIX 272..281
FT /evidence="ECO:0007829|PDB:1HT6"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:1HT6"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:1HT6"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:1HT6"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:1HT6"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:1HT6"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:1HT6"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:1HT6"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:1HT6"
FT HELIX 330..339
FT /evidence="ECO:0007829|PDB:1HT6"
FT STRAND 340..347
FT /evidence="ECO:0007829|PDB:1HT6"
FT HELIX 348..352
FT /evidence="ECO:0007829|PDB:1HT6"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:3BSH"
FT HELIX 357..369
FT /evidence="ECO:0007829|PDB:1HT6"
FT STRAND 378..384
FT /evidence="ECO:0007829|PDB:1HT6"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:1HT6"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:1HT6"
FT STRAND 396..402
FT /evidence="ECO:0007829|PDB:1HT6"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:1HT6"
FT STRAND 415..420
FT /evidence="ECO:0007829|PDB:1HT6"
FT STRAND 423..427
FT /evidence="ECO:0007829|PDB:1HT6"
SQ SEQUENCE 438 AA; 47796 MW; 2393FDAC51E80F51 CRC64;
MGKNGSLCCF SLLLLLLLAG LASGHQVLFQ GFNWESWKQS GGWYNMMMGK VDDIAAAGVT
HVWLPPPSHS VSNEGYMPGR LYDIDASKYG NAAELKSLIG ALHGKGVQAI ADIVINHRCA
DYKDSRGIYC IFEGGTSDGR LDWGPHMICR DDTKYSDGTA NLDTGADFAA APDIDHLNDR
VQRELKEWLL WLKSDLGFDA WRLDFARGYS PEMAKVYIDG TSPSLAVAEV WDNMATGGDG
KPNYDQDAHR QNLVNWVDKV GGAASAGMVF DFTTKGILNA AVEGELWRLI DPQGKAPGVM
GWWPAKAATF VDNHDTGSTQ AMWPFPSDKV MQGYAYILTH PGIPCIFYDH FFNWGFKDQI
AALVAIRKRN GITATSALKI LMHEGDAYVA EIDGKVVVKI GSRYDVGAVI PAGFVTSAHG
NDYAVWEKNG AAATLQRS
