ID   AMY1_AERHY              Reviewed;         464 AA.
AC   P22630;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Alpha-amylase;
DE            EC=3.2.1.1;
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE   Flags: Precursor;
OS   Aeromonas hydrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=JMP636;
RX   PubMed=2449422; DOI=10.1128/jb.170.3.1325-1332.1988;
RA   Gobius K.S., Pemberton J.M.;
RT   "Molecular cloning, characterization, and nucleotide sequence of an
RT   extracellular amylase gene from Aeromonas hydrophila.";
RL   J. Bacteriol. 170:1325-1332(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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; M20401; AAA21936.1; -; Genomic_DNA.
DR   PIR; A28631; A28631.
DR   AlphaFoldDB; P22630; -.
DR   SMR; P22630; -.
DR   STRING; 1448139.AI20_12680; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   eggNOG; COG0366; Bacteria.
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   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..464
FT                   /note="Alpha-amylase"
FT                   /id="PRO_0000001326"
FT   ACT_SITE        215
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        242
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         218..219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         313
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            314
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   464 AA;  51656 MW;  E82A3298EEAC5C49 CRC64;
     MKNTAGILAI AGMLIAPLAH ADVILHAFNW KYSEVTAKAD LIKGAGYKQV LISPPLKSSG
     NEWWARYQPQ DLRLVDSPLG NKQDLEQLIA AMQARGIAVY ADVVLNHMAN ESWKRNDLNY
     PGTELLGQYA ANPDYYSRQR LFGDLGQNLL SASDFHPEGC ITDWSDPGHV QYWRLCGGAG
     DKGLPDLDPN NWVVSQQQAY LKALKGMGIK GFRVDAVKHM SDYQINAVFT PEIKQGMHVF
     GEVITTGGAG STDYERFLKP YLDNSGQGAY DFPLFASLRG ALGYGGSMNQ LADPGAYGQA
     LPGNRAVTFA ITHDIPTNDG FRYQILNQTD EKLAYAYLLG RDGGSPLVYS DHGETQDKDG
     LRWQDYYLRS DLKGMIRFHN AVQGQPMQLI GSGDCFVLFK RGKQGLVGVN KCDYEQEYWL
     DTAKFELNWY RNYKDVLDQS AVINVQSQWV RVAMPARRPP LAAE