ID   AMY_STRTL               Reviewed;         460 AA.
AC   P27350;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Alpha-amylase;
DE            EC=3.2.1.1;
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE   Flags: Precursor;
GN   Name=amy;
OS   Streptomyces thermoviolaceus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CUB74;
RX   PubMed=8486279; DOI=10.1016/0378-1119(93)90628-g;
RA   Bahri S.M., Ward J.M.;
RT   "Sequence of the Streptomyces thermoviolaceus CUB74 alpha-amylase-encoding
RT   gene and its transcription analysis in Streptomyces lividans.";
RL   Gene 127:133-137(1993).
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; M34957; AAA26697.1; -; Genomic_DNA.
DR   PIR; JN0663; JN0663.
DR   AlphaFoldDB; P27350; -.
DR   SMR; P27350; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..460
FT                   /note="Alpha-amylase"
FT                   /id="PRO_0000001343"
FT   ACT_SITE        206
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        233
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         210
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            297
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   460 AA;  49873 MW;  40071FEA7DC02B22 CRC64;
     MASRTLSGAL ALAAAATAVL AAPATVAHRS PPGTKDVTAV LFEWDYVSVA KECTSTLGPA
     GYGYVQVSPP AEHIQGSQWW TSYQPVSYKI AGRLGDRAAF RSMVNTCHAA GVKVVVDTVI
     NHMSAGSGTG TGGSSYTKYD YPGLYSAPDF DDCTAEITDY QDRWNVQHCE LVGLADLDTG
     EEYVRQTIAG YMNDLLSLGV DGFRIDAATH IPAEDLANIK SRLSNPNAYW KQEVIYGAGE
     PPKPGEYTGT GDVQEFRYAY DLKRVFTQEH LAYLKNYGED WGYLSSTTAG VFVDNHDTER
     NGSTLNYKND ATYTLANVFM LAWPYGAPDI NSGYEWSDPD ARPPDGGHVD ACWQNGWKCQ
     HKWPEIASMV AFRNATRGEP VTDWWDDGAD AIAFGRGSKG FVAINHESAT VQRTYQTSLP
     AGTYCDVQSN TTVTVDSAGR FTAALGPDTA LALHNGRTSC