ID   AMY_NIACI               Reviewed;         528 AA.
AC   P08137;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Alpha-amylase;
DE            EC=3.2.1.1;
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE   Flags: Precursor;
OS   Niallia circulans (Bacillus circulans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Niallia.
OX   NCBI_TaxID=1397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3109866; DOI=10.1089/dna.1987.6.255;
RA   Nishizawa M., Ozawa F., Hishinuma F.;
RT   "Molecular cloning of an amylase gene of Bacillus circulans.";
RL   DNA 6:255-265(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; M16657; AAA22229.1; -; Genomic_DNA.
DR   PIR; A29083; ALBSK.
DR   AlphaFoldDB; P08137; -.
DR   SMR; P08137; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR013777; A-amylase-like.
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   PIRSF; PIRSF001024; Alph-amyl_fung; 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..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..528
FT                   /note="Alpha-amylase"
FT                   /id="PRO_0000001331"
FT   ACT_SITE        258
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        286
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         262
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            357
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   528 AA;  57941 MW;  455740202FA29753 CRC64;
     MNKKWLNIPA LIALLAAIAF GSVAPAEAAP ATSVSNKQNF STDVIYQIVT DRFVDGNTAN
     NPAGSAYDAT CSTNLKLYCG GDWQGIMNKI NDGYFTGMGI TALWISQPVE NIYSVINYSG
     VNNTAYHGYW ARDFKKTNPA FGSMTDFANL ISAAHSRNIK VVIDFAPNHT SPAMETNASF
     GENGKLYDNG TLLGGYTGDT NGYFHHNGGT DFSTLKNGIY KNLYDLADLN HNNSTIDTYF
     KNAIRLWLDM GIDGIRVDAV KHMPFGWQKN WMSSIYSYKP VFTFGEWFLG TNETDANNTY
     FANESGMSLL DFRFSQKVRQ VFRDGSDTMY GLDSMLSSTA ADYYSVNDQV TFLDNHDMDR
     FQVSGANGRK LEQALALTLT SRGVPAIYYG TEQYMTGNGD PNNRAKMSSF STSTTAYNVI
     SKLAPLRKSN PAIAYGTTQQ RWINNDVYIY ERKFGNNVAV VAINKNLTSS YSIAGLNTSL
     PSGTYTDVLA NSLSGNSITV GSSGAVNTFT LQAGGEASGL TRRRQRLR