AMY2_HORVU
ID AMY2_HORVU Reviewed; 427 AA.
AC P04063;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 3.
DT 03-AUG-2022, entry version 137.
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=AMY2-2;
DE AltName: Full=High pI alpha-amylase;
DE Flags: Precursor;
GN Name=AMY1.2;
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 [GENOMIC DNA].
RA Rahmatullah R.J., Huang J.K., Clark K.L., Reeck G.R., Chandra G.R.,
RA Muthukrishnan S.;
RT "Nucleotide and predicted amino acid sequences of two different genes for
RT high-pI alpha-amylases from barley.";
RL Plant Mol. Biol. 12:119-121(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3871776; DOI=10.1016/s0021-9258(19)83685-2;
RA Rogers J.C.;
RT "Two barley alpha-amylase gene families are regulated differently in
RT aleurone cells.";
RL J. Biol. Chem. 260:3731-3738(1985).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 25-427 IN COMPLEX WITH CALCIUM,
RP AND COFACTOR.
RX PubMed=8196040; DOI=10.1006/jmbi.1994.1354;
RA Kadziola A., Abe J.-I., Svensson B., Haser R.;
RT "Crystal and molecular structure of barley alpha-amylase.";
RL J. Mol. Biol. 239:104-121(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 25-427 IN COMPLEX WITH CALCIUM
RP IONS AND ACARBOSE, ACTIVE SITE, AND COFACTOR.
RX PubMed=9571044; DOI=10.1006/jmbi.1998.1683;
RA Kadziola A., Sogaard M., Svensson B., Haser R.;
RT "Molecular structure of a barley alpha-amylase-inhibitor complex:
RT implications for starch binding and catalysis.";
RL J. Mol. Biol. 278:205-217(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH BASI AND CALCIUM
RP IONS, AND COFACTOR.
RC STRAIN=cv. Menuet;
RX PubMed=9634702; DOI=10.1016/s0969-2126(98)00066-5;
RA Vallee F., Kadziola A., Bourne Y., Juy M., Rodenburg K.W., Svensson B.,
RA Haser R.;
RT "Barley alpha-amylase bound to its endogenous protein inhibitor BASI:
RT crystal structure of the complex at 1.9-A resolution.";
RL Structure 6:649-659(1998).
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:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044,
CC ECO:0000269|PubMed:9634702};
CC Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000269|PubMed:8196040,
CC ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8196040,
CC ECO:0000269|PubMed:9571044}.
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 -!- INDUCTION: Type B isozyme mRNA is undetectable in unstimulated cells
CC and increases a hundred-fold after stimulation with gibberellic acid.
CC -!- MISCELLANEOUS: There are at least 4 types of alpha-amylase in barley.
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; X15226; CAA33298.1; -; Genomic_DNA.
DR EMBL; K02637; AAA98790.1; -; Genomic_DNA.
DR PIR; A31960; ALBHB.
DR PDB; 1AMY; X-ray; 2.80 A; A=25-427.
DR PDB; 1AVA; X-ray; 1.90 A; A/B=25-427.
DR PDB; 1BG9; X-ray; 2.80 A; A=25-427.
DR PDBsum; 1AMY; -.
DR PDBsum; 1AVA; -.
DR PDBsum; 1BG9; -.
DR AlphaFoldDB; P04063; -.
DR SMR; P04063; -.
DR DIP; DIP-6097N; -.
DR IntAct; P04063; 1.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; P04063; -.
DR EnsemblPlants; HORVU.MOREX.r2.6HG0512110.1; HORVU.MOREX.r2.6HG0512110.1; HORVU.MOREX.r2.6HG0512110.
DR Gramene; HORVU.MOREX.r2.6HG0512110.1; HORVU.MOREX.r2.6HG0512110.1; HORVU.MOREX.r2.6HG0512110.
DR BRENDA; 3.2.1.1; 2687.
DR EvolutionaryTrace; P04063; -.
DR ExpressionAtlas; P04063; 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: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; Signal.
FT SIGNAL 1..24
FT CHAIN 25..427
FT /note="Alpha-amylase type B isozyme"
FT /id="PRO_0000001405"
FT ACT_SITE 203
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:9571044"
FT ACT_SITE 228
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:9571044"
FT BINDING 75..76
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:9571044"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:8196040,
FT ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702,
FT ECO:0007744|PDB:1AVA"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:8196040,
FT ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702,
FT ECO:0007744|PDB:1AVA"
FT BINDING 135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:8196040,
FT ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702,
FT ECO:0007744|PDB:1AVA"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:8196040,
FT ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702,
FT ECO:0007744|PDB:1AVA"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:8196040,
FT ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702,
FT ECO:0007744|PDB:1AVA"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:8196040,
FT ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702,
FT ECO:0007744|PDB:1AVA"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:8196040,
FT ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702,
FT ECO:0007744|PDB:1AVA"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:8196040,
FT ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702,
FT ECO:0007744|PDB:1AVA"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:8196040,
FT ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702,
FT ECO:0007744|PDB:1AVA"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:8196040,
FT ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702,
FT ECO:0007744|PDB:1AVA"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:8196040,
FT ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702,
FT ECO:0007744|PDB:1AVA"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:8196040,
FT ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702,
FT ECO:0007744|PDB:1AVA"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:8196040,
FT ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702,
FT ECO:0007744|PDB:1AVA"
FT BINDING 201..206
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:9571044"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:8196040,
FT ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702,
FT ECO:0007744|PDB:1AVA"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:9571044"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:9571044"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:9571044"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:9571044"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 299..301
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:9571044"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:9571044"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 414..420
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 424
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT SITE 313
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:9571044"
FT CONFLICT 134
FT /note="G -> D (in Ref. 1; CAA33298)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="E -> Q (in Ref. 1; CAA33298)"
FT /evidence="ECO:0000305"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1AVA"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1AVA"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:1AVA"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1AVA"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1AMY"
FT HELIX 91..104
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:1AVA"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1AVA"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1AMY"
FT HELIX 178..193
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:1AVA"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:1AVA"
FT HELIX 210..220
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:1AVA"
FT HELIX 246..260
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:1AVA"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:1AVA"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:1AVA"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:1AVA"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:1AVA"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:1AVA"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:1AVA"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:1AVA"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:1AVA"
FT HELIX 328..337
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 338..345
FT /evidence="ECO:0007829|PDB:1AVA"
FT HELIX 346..350
FT /evidence="ECO:0007829|PDB:1AVA"
FT HELIX 355..367
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:1AVA"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 394..400
FT /evidence="ECO:0007829|PDB:1AVA"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 410..418
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 421..426
FT /evidence="ECO:0007829|PDB:1AVA"
SQ SEQUENCE 427 AA; 47356 MW; 957C0B16621BF748 CRC64;
MANKHLSLSL FLVLLGLSAS LASGQVLFQG FNWESWKHNG GWYNFLMGKV DDIAAAGITH
VWLPPASQSV AEQGYMPGRL YDLDASKYGN KAQLKSLIGA LHGKGVKAIA DIVINHRTAE
HKDGRGIYCI FEGGTPDARL DWGPHMICRD DRPYADGTGN PDTGADFGAA PDIDHLNLRV
QKELVEWLNW LKADIGFDGW RFDFAKGYSA DVAKIYIDRS EPSFAVAEIW TSLAYGGDGK
PNLNQDQHRQ ELVNWVDKVG GKGPATTFDF TTKGILNVAV EGELWRLRGT DGKAPGMIGW
WPAKAVTFVD NHDTGSTQHM WPFPSDRVMQ GYAYILTHPG TPCIFYDHFF DWGLKEEIDR
LVSVRTRHGI HNESKLQIIE ADADLYLAEI DGKVIVKLGP RYDVGNLIPG GFKVAAHGND
YAVWEKI
