AMYB_WHEAT
ID AMYB_WHEAT Reviewed; 503 AA.
AC P93594;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Beta-amylase Tri a 17 {ECO:0000303|Ref.1};
DE EC=3.2.1.2 {ECO:0000269|PubMed:30515829};
DE AltName: Full=1,4-alpha-D-glucan maltohydrolase;
DE AltName: Allergen=Tri a 17.0101 {ECO:0000305};
GN Name=BMY1; Synonyms=AMY1;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Star; TISSUE=Leaf;
RA Wagner G.B., Haeger K.-P., Ziegler P.;
RT "Nucleotide sequence of a cDNA from wheat leaves encoding ubiquitous beta-
RT amylase.";
RL (er) Plant Gene Register PGR96-123(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ALLERGEN, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=30515829; DOI=10.1111/all.13696;
RA Hofer G., Wieser S., Bogdos M.K., Gattinger P., Nakamura R., Ebisawa M.,
RA Maekelae M., Papadopoulos N., Valenta R., Keller W.;
RT "Three-dimensional structure of the wheat beta-amylase Tri a 17, a
RT clinically relevant food allergen.";
RL Allergy 74:1009-1013(2019).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides so as to remove successive maltose units from the
CC non-reducing ends of the chains.; EC=3.2.1.2;
CC Evidence={ECO:0000269|PubMed:30515829};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5. Highly active at acidic pH range 4-7. Retains over
CC 80% of maximum activity at 4.0. At higher pH values the activity
CC decreases markedly, with more than 50% of activity lost at pH 8.0.
CC {ECO:0000269|PubMed:30515829};
CC -!- ALLERGEN: Causes an allergic reaction in human. Recombinant protein
CC binds to IgE in 41% of the 17 European wheat food-allergic patients
CC tested. Six of these patients have a history of wheat-induced
CC anaphylaxis. Estimation by logistic regression indicates a 24-fold
CC higher probability of the relative risk of beta-amylase-reactive
CC patients to develop a wheat-induced anaphylaxis. Induces degranulation
CC of the humanized rat basophilic leukemia (RBL) cells and releases
CC hexosaminidase from them. {ECO:0000269|PubMed:30515829}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family. {ECO:0000305}.
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DR EMBL; X98504; CAA67128.1; -; mRNA.
DR PDB; 6GER; X-ray; 2.00 A; A=1-503.
DR PDBsum; 6GER; -.
DR AlphaFoldDB; P93594; -.
DR SMR; P93594; -.
DR STRING; 4565.Traes_2DS_D14ABD1DB.1; -.
DR Allergome; 12172; Tri a 17.0101.
DR Allergome; 9594; Tri a 17.
DR CAZy; GH14; Glycoside Hydrolase Family 14.
DR PRIDE; P93594; -.
DR EnsemblPlants; TraesCAD_scaffold_006468_01G000300.1; TraesCAD_scaffold_006468_01G000300.1; TraesCAD_scaffold_006468_01G000300.
DR EnsemblPlants; TraesCLE_scaffold_004113_01G000300.1; TraesCLE_scaffold_004113_01G000300.1; TraesCLE_scaffold_004113_01G000300.
DR EnsemblPlants; TraesCS2D02G220900.3; TraesCS2D02G220900.3; TraesCS2D02G220900.
DR EnsemblPlants; TraesPAR_scaffold_025646_01G000100.1; TraesPAR_scaffold_025646_01G000100.1; TraesPAR_scaffold_025646_01G000100.
DR EnsemblPlants; TraesROB_scaffold_013018_01G000100.1; TraesROB_scaffold_013018_01G000100.1; TraesROB_scaffold_013018_01G000100.
DR EnsemblPlants; TraesWEE_scaffold_004902_01G000300.1; TraesWEE_scaffold_004902_01G000300.1; TraesWEE_scaffold_004902_01G000300.
DR Gramene; TraesCAD_scaffold_006468_01G000300.1; TraesCAD_scaffold_006468_01G000300.1; TraesCAD_scaffold_006468_01G000300.
DR Gramene; TraesCLE_scaffold_004113_01G000300.1; TraesCLE_scaffold_004113_01G000300.1; TraesCLE_scaffold_004113_01G000300.
DR Gramene; TraesCS2D02G220900.3; TraesCS2D02G220900.3; TraesCS2D02G220900.
DR Gramene; TraesPAR_scaffold_025646_01G000100.1; TraesPAR_scaffold_025646_01G000100.1; TraesPAR_scaffold_025646_01G000100.
DR Gramene; TraesROB_scaffold_013018_01G000100.1; TraesROB_scaffold_013018_01G000100.1; TraesROB_scaffold_013018_01G000100.
DR Gramene; TraesWEE_scaffold_004902_01G000300.1; TraesWEE_scaffold_004902_01G000300.1; TraesWEE_scaffold_004902_01G000300.
DR eggNOG; ENOG502QUU5; Eukaryota.
DR OMA; KECGMKM; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P93594; baseline and differential.
DR GO; GO:0102229; F:amylopectin maltohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016161; F:beta-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR001554; Glyco_hydro_14.
DR InterPro; IPR018238; Glyco_hydro_14_CS.
DR InterPro; IPR001371; Glyco_hydro_14B_pln.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31352; PTHR31352; 1.
DR Pfam; PF01373; Glyco_hydro_14; 1.
DR PRINTS; PR00750; BETAAMYLASE.
DR PRINTS; PR00842; GLHYDLASE14B.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00506; BETA_AMYLASE_1; 1.
DR PROSITE; PS00679; BETA_AMYLASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome.
FT CHAIN 1..503
FT /note="Beta-amylase Tri a 17"
FT /id="PRO_0000153941"
FT ACT_SITE 184
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10050"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 379..380
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 418
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:6GER"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 30..42
FT /evidence="ECO:0007829|PDB:6GER"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 68..79
FT /evidence="ECO:0007829|PDB:6GER"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:6GER"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:6GER"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 148..162
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:6GER"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 209..221
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:6GER"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 255..282
FT /evidence="ECO:0007829|PDB:6GER"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:6GER"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:6GER"
FT TURN 299..302
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 307..312
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 324..331
FT /evidence="ECO:0007829|PDB:6GER"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:6GER"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 357..370
FT /evidence="ECO:0007829|PDB:6GER"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 386..396
FT /evidence="ECO:0007829|PDB:6GER"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 421..424
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 426..439
FT /evidence="ECO:0007829|PDB:6GER"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:6GER"
FT HELIX 464..469
FT /evidence="ECO:0007829|PDB:6GER"
SQ SEQUENCE 503 AA; 56611 MW; 71E9E1533A6C0F73 CRC64;
MAGNMLANYV QVYVMLPLDV VSVDNKFEKG DEIRAQLKKL TEAGVDGVMI DVWWGLVEGK
GPKAYDWSAY KQVFDLVHEA GLKLQAIMSF HQCGGNVGDV VNIPIPQWVR DVGATDPDIF
YTNRGGTRNI EYLTLGVDDQ PLFHGRTAVQ MYADYMASFR ENMKKFLDAG TIVDIEVGLG
PAGEMRYPSY PQSQGWVFPG IGEFICYDKY LEADFKAAAA KAGHPEWELP DDAGEYNDTP
EKTQFFKDNG TYLTEKGKFF LSWYSNKLIK HGDKILDEAN KVFLGCRVQL AIKISGIHWW
YRVPNHAAEL TAGYYNLDDR DGYRTIARML TRHHASMNFT CAEMRDSEQS EEAKSAPEEL
VQQVLSAGWR EGLHVACENA LGRYDATAYN TILRNARPKG INKNGPPEHK LFGFTYLRLS
NELLEGQNYA TFQTFVEKMH ANLGHDPSVD PVAPLERSKP EMPIEMILKA AQPKLEPFPF
DKNTDLPVKD HTDVGDEVLV APV
