ID   AMYA_AERHY              Reviewed;         443 AA.
AC   P41131;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=amyA;
OS   Aeromonas hydrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MCC-1;
RX   PubMed=8126440; DOI=10.1099/00221287-139-12-3215;
RA   Chang M.C., Chang J.C., Chen J.P.;
RT   "Cloning and nucleotide sequence of an extracellular alpha-amylase gene
RT   from Aeromonas hydrophila MCC-1.";
RL   J. Gen. Microbiol. 139:3215-3223(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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; L19299; AAA21016.1; -; Genomic_DNA.
DR   PIR; I39538; I39538.
DR   AlphaFoldDB; P41131; -.
DR   SMR; P41131; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1180; -; 1.
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   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..443
FT                   /note="Alpha-amylase"
FT                   /id="PRO_0000001327"
FT   ACT_SITE        198
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        223
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         201..202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            288
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   443 AA;  48333 MW;  8F8D60B9341A92F9 CRC64;
     MHNTLFRTAL LAAALGSFSH TASAEGVMVH LFEWKFNDIA NECETVLGPK GFGGVQVSPP
     AEHKQGSQVW WTVYQPVSYK NFNSFGGCEA ELRSMIARCN AAGVKVYADA VFNHMASGSG
     TATGGGSYNS GQYQYPQFGY NDFHHSGDIT NYGDSNNVWN GALYGLPDLN TGSSYVQDQI
     ATYMKTLLGW GVAGFRIDAA KHMAPADVKA ILDKAGSPRA YLEVIGAGGE SPDIQPGRYT
     YIDTVTEFKY GTDLAANFNG QIKNLKTLGE SWGLLPSNKA FVFVDNHDPE RAHGGGGMLT
     FMQGARYDLA NTFMLAWPYG WKQVMSAYRF ENMGTYETDK GAPGSTPCTD SQWNCEQRRP
     TIMNMVLFRN RTEGQPVSNW WDNGNNQIAF SRGTRASSPS TTRAARWWPR CRRSRPASTA
     TSWGAMTTAA AVMSPSTAAA RPA