ID   AMY_STRHY               Reviewed;         478 AA.
AC   P08486;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Alpha-amylase;
DE            EC=3.2.1.1;
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE   Flags: Precursor;
OS   Streptomyces hygroscopicus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=1912;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3029013; DOI=10.1128/jb.169.3.1029-1036.1987;
RA   Hoshiko S., Makabe O., Nojiri C., Katsumata K., Satoh E., Nagaoka K.;
RT   "Molecular cloning and characterization of the Streptomyces hygroscopicus
RT   alpha-amylase gene.";
RL   J. Bacteriol. 169:1029-1036(1987).
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; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; M15540; AAA26698.1; -; Genomic_DNA.
DR   AlphaFoldDB; P08486; -.
DR   SMR; P08486; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; P08486; -.
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; 2.60.40.1180; -; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR031319; A-amylase_C.
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; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Calcium; Carbohydrate metabolism; Glycosidase; Hydrolase; Metal-binding;
KW   Signal.
FT   SIGNAL          1..30
FT   CHAIN           31..478
FT                   /note="Alpha-amylase"
FT                   /id="PRO_0000001341"
FT   ACT_SITE        204
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        230
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            292
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   478 AA;  50755 MW;  FC7B0AF9C6F22F4F CRC64;
     MQQRSRVLGG TLAGIVAAAA ATVAPWPSQA TPPGQKTVTA TLFERKYVDV AKACTDQLGP
     AGYGYVEVSP ASEHIQGGQW WTSYQPVSYK IAGRLGDRDA FASMVSACHA AGVKVIADAV
     VNHMAAGSGR HHAQYTKYNY PGFYQDQTFH GCRKSISDYT NRDDVQTCEL VDLADLGTGS
     DYVRTTIAGY LGLRSLGVDG FRIDAAKHIS ATDLAAVKGK MKDPGFWVQE VIYGAGEAVR
     PDEYTGIGDV DEFRYGTHLK SAFQSGNIAQ LKSVADGKLW QRQARTFVDN WDTERNGSTL
     TYKDGAAYTL ANVFMLASPY GSPNVYSGYE WTDKDAAAGG STGWTDDAAK REITGMVGFR
     NAVGSAELTN WWDNGGRPLA FARSDKGFVA LNNGDAALTQ TFATSLPAGT YCDVVHAASS
     CDGDTVTVGD TEAQVDAAKS VALHVGATGQ SACRQAVALH VPGQSAGSPR SSAKRVEQ