AMY4_HORVU
ID AMY4_HORVU Reviewed; 153 AA.
AC P04748;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Alpha-amylase type B isozyme;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P00693};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE AltName: Full=Clone 103;
DE Flags: Fragment;
GN Name=AMY1.4;
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].
RX PubMed=6335720;
RA Huang J.-K., Swegle M., Dandekar A.M., Muthukrishnan S.;
RT "Expression and regulation of alpha-amylase gene family in barley
RT aleurones.";
RL J. Mol. Appl. Genet. 2:579-588(1984).
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:0000250|UniProtKB:P00693};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P00693};
CC Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:P00693};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
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: Type B isozyme mRNA is undetectable in unstimulated
CC cells and increases a hundred-fold after stimulation with gibberellic
CC acid.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; M10056; AAA32930.1; -; mRNA.
DR PIR; A21826; A21826.
DR AlphaFoldDB; P04748; -.
DR SMR; P04748; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR ExpressionAtlas; P04748; baseline.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0044275; P:cellular carbohydrate catabolic process; IEA:UniProt.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR012850; A-amylase_bs_C.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF07821; Alpha-amyl_C2; 1.
DR SMART; SM00810; Alpha-amyl_C2; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 2: Evidence at transcript level;
KW Calcium; Carbohydrate metabolism; Germination; Glycosidase; Hydrolase.
FT CHAIN <1..153
FT /note="Alpha-amylase type B isozyme"
FT /id="PRO_0000054292"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 25..27
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT SITE 39
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT NON_TER 1
SQ SEQUENCE 153 AA; 17276 MW; BE5233AE1D265F72 CRC64;
ILNVAVEGAL WRLRGTDGKA PSMIGWWPAK AVTFVDNHDT GSTQHMWPFP SDRVMQGYAY
ILTHPRTPCI FYDHFFDWGP KEEIDRLVSV RTRHGIHNES KLQIIEADAD LYLAEIDGKV
IVKLGPRYDV GNLIPGGFEG AAHGNDYAVW EKI
