ID   AMY_STRVL               Reviewed;         569 AA.
AC   P22998;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=aml;
OS   Streptomyces violaceus (Streptomyces venezuelae).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1936;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15068 / DSM 41111 / IMRU 3629;
RX   PubMed=3266752; DOI=10.1016/0378-1119(88)90166-7;
RA   Virolle M.-J., Long C.M., Chang S., Bibb M.J.;
RT   "Cloning, characterisation and regulation of an alpha-amylase gene from
RT   Streptomyces venezuelae.";
RL   Gene 74:321-334(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; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- INDUCTION: By maltose, and repression by glucose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; M25263; AAB36561.1; -; Genomic_DNA.
DR   PIR; JS0101; JS0101.
DR   AlphaFoldDB; P22998; -.
DR   SMR; P22998; -.
DR   CAZy; CBM20; Carbohydrate-Binding Module Family 20.
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:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
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; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR002044; CBM_fam20.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SMART; SM01065; CBM_2; 1.
DR   SUPFAM; SSF49452; SSF49452; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51166; CBM20; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Carbohydrate metabolism; Glycosidase; Hydrolase; Metal-binding;
KW   Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..569
FT                   /note="Alpha-amylase"
FT                   /id="PRO_0000001344"
FT   DOMAIN          468..569
FT                   /note="CBM20"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT   ACT_SITE        205
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        232
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
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         209
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            296
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   569 AA;  60637 MW;  14CA5B1D56720043 CRC64;
     MARKTVAAAL ALVAGAAVAV TGNAPAQAVP PGEKDVTAVM FEWNFASVAR ECTDRLGPAG
     YGYVQVSPPQ EHLQGGQWWT SYQPVSYKIA GRLGDRTAFK NMIDTCHAAG VKVVADSVIN
     HMANGSGTGT GGTSFSKYDY PGLYSGSDMD DCRATISNYQ DRANVQNCEL VQLPDLDTGE
     DHVRGKIAGY LNDLASLGVD GFRIDAAKHM PAADLANIKS RLTNPNVFWK LEAIHGAGEA
     VSPSEYLGSG DVQEFRYARD LKRVLQGEKL SYLKNFGEAW GHMPSGQSGV FVDNHDTERG
     GDTLSYKDGA NYTLASVFML AWPYGSPDVH SGYEWTDKDA GPPNNGQVNA CYTDGWKCQH
     AWREISSMVA FRNTARGQAV TNWWDNGNNA IAFGRGSKAY VAINHETSAL TRTFQTSLPA
     GSYCDVQSNT PVTVNSSGQF TATLAANTAV ALHVNATGCG STPTTPPTTP PATSGASFNV
     TATTVVGQNI YVTGNRAELG NWAPASALKL DPATYPVWKL TVGLPAGTSF EYKYIRKDAA
     GNVTWESGAN RTATVPASGQ LVLNDTFRS