ID   AMY_PRIMG               Reviewed;         520 AA.
AC   P20845;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Alpha-amylase;
DE            EC=3.2.1.1;
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE   Flags: Precursor;
OS   Priestia megaterium (Bacillus megaterium).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=1404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2455281; DOI=10.1093/nar/16.11.5203;
RA   Metz R.J., Allen L.N., Cao T.M., Zeman N.W.;
RT   "Nucleotide sequence of an amylase gene from Bacillus megaterium.";
RL   Nucleic Acids Res. 16:5203-5203(1988).
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;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:Q8A1G3};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8A1G3};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; X07261; CAA30247.1; -; Genomic_DNA.
DR   PIR; S01031; S01031.
DR   AlphaFoldDB; P20845; -.
DR   SMR; P20845; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   BRENDA; 3.2.1.1; 656.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.400.10; -; 1.
DR   InterPro; IPR022567; DUF3459.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045857; O16G_dom_2.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF11941; DUF3459; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Calcium; Carbohydrate metabolism; Direct protein sequencing; Glycosidase;
KW   Hydrolase; Metal-binding; Signal.
FT   SIGNAL          1..27
FT   CHAIN           28..520
FT                   /note="Alpha-amylase"
FT                   /id="PRO_0000001333"
FT   ACT_SITE        233
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        273
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q8A1G3"
FT   BINDING         203
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q8A1G3"
FT   BINDING         237
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q8A1G3"
FT   SITE            340
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   520 AA;  58761 MW;  2C649D957F5835C0 CRC64;
     MKGKKWTALA LTLPLAASLS TGVDAETVHK GKAPTADKNG VFYEVYVNSF YDANKDGHGD
     LKGLTQKLDY LNDGNSHTKN DLQVNGIWMM PVNPSPSYHK YDVTDYYNID PQYGNLQDFR
     KLMKEADKRD VKVIMDLVVN HTSSEHPWFQ AALKDKNSKY RDYYIWADKN TDLNEKGSWG
     QQVWHKAPNG EYFYGTFWEG MPDLNYDNPE VRKEMINVGK FWLKQGVDGF RLDAALHIFK
     GQTPEGAKKN ILWWNEFRDA MKKENPNVYL TGEVWDQPEV VAPYYQSLDS LFNFDLAGKI
     VSSVKAGNDQ GIATAAAATD ELFKSYNPNK IDGIFLTNHD QNRVMSELSG DVNKAKSAAS
     ILLTLPGNPY IYYGEEIGMT GEKPDELIRE PFRWYEGNGI GQTSWETPVY NKGGNGVSVE
     AQTKQKDSLL NHYREMIRVR QQHEELVKGT LQSISVDSKE VVAYSRTYKG KSISVYHNIS
     NQPVKVSVAA KGNLIFASEK GAKKVKNQLV IPANRTVLIK