AMY5_HORVU
ID AMY5_HORVU Reviewed; 135 AA.
AC P04749;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 110.
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 168;
DE Flags: Fragment;
GN Name=AMY1.5;
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; K02635; AAA32931.1; -; mRNA.
DR PIR; C21826; C21826.
DR AlphaFoldDB; P04749; -.
DR SMR; P04749; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
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..135
FT /note="Alpha-amylase type B isozyme"
FT /id="PRO_0000054293"
FT BINDING 1
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 7..9
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 26
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT SITE 21
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT NON_TER 1
SQ SEQUENCE 135 AA; 15140 MW; 947F71F5E13DD2A6 CRC64;
KAPGMIGWWP AKAVTFVNNH DTGSTQHMWP FPSDRVMQGY AYILTHQGTP CIFYDHFFDW
GPKEEIDRLV SVSTRHGIHS ESKLQIIEAD ADLCLAEIDG KVIVKLGPRY DVGNLIPGGF
EVAAHGNDYA VWEKI
