ID   AMY_STRGR               Reviewed;         566 AA.
AC   P30270;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 101.
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 griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IMRU 3570;
RX   PubMed=1900915; DOI=10.1007/bf00269860;
RA   Vigal T., Gil J.A., Daza A., Garcia-Gonzalez M.D., Martin J.F.;
RT   "Cloning, characterization and expression of an alpha-amylase gene from
RT   Streptomyces griseus IMRU3570.";
RL   Mol. Gen. Genet. 225:278-288(1991).
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; X57568; CAA40798.1; -; Genomic_DNA.
DR   PIR; S14063; S14063.
DR   AlphaFoldDB; P30270; -.
DR   SMR; P30270; -.
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   3: Inferred from homology;
KW   Calcium; Carbohydrate metabolism; Glycosidase; Hydrolase; Metal-binding;
KW   Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000250"
FT   CHAIN           29..566
FT                   /note="Alpha-amylase"
FT                   /id="PRO_0000001340"
FT   DOMAIN          465..566
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   566 AA;  59706 MW;  FCBAA7B172A617C7 CRC64;
     MARRLATASL AVLAAAATAL TAPTPAAAAP PGAKDVTAVL FEWKFASVAR ACTDSLGPAG
     YGYVQVSPPQ EHIQGSQWWT SYQPVSYKIA GRLGDRAAFK SMVDTCHAAG VKVVADSVIN
     HMAAGSGTGT GGSAYQKYDY PGIWSGADMD DCRSEINDYG NRANVQNCEL VGLADLDTGE
     PYVRDRIAAY LNDLLLLGVD GFRIDAAKHM PAADLTAIKA KVGNGSTYWK QEAIHGAGEA
     VQPSEYLGTG DVQEFRYARD LKRVFQNENL AHLKNFGEDW GYMASGKSAV FVDNHDTERG
     GDTLNYKNGS AYTLAGVFML AWPYGSPDVH SGYEFTDHDA GPPNGGTVNA CYSDGWKCQH
     AWPELSSMVG LRNTASGQPV TNWWDNGGDQ IAFGRGDKAY VAINHEGSAL NRTFQSGLPG
     GAYCDVQSGR SVTVGSDGTF TATVAAGTAL ALHTGARTCS GGGTGPGTGQ TSASFHVNAT
     TAWGENIYVT GDQAALGNWD PARALKLDPA AYPVWKLDVP LAAGTPFQYK YLRKDAAGKA
     VWESGANRTA TVGTTGALTL NDTWRG