ID   AMY_PECMA               Reviewed;         508 AA.
AC   P91778;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Alpha-amylase;
DE            EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE   Flags: Precursor;
OS   Pecten maximus (King scallop) (Pilgrim's clam).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae; Pecten.
OX   NCBI_TaxID=6579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Digestive gland;
RX   PubMed=9284561;
RA   Le Moine S., Sellos D., Moal J., Daniel J.Y., San Juan Serrano F.,
RA   Samain J.F., Van Wormhoudt A.;
RT   "Amylase on Pecten maximus (Mollusca, bivalves): protein and cDNA
RT   characterization; quantification of the expression in the digestive
RT   gland.";
RL   Mol. Mar. Biol. Biotechnol. 6:228-237(1997).
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; Evidence={ECO:0000250|UniProtKB:P04746};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P04746};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P04746};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000250|UniProtKB:P04746};
CC       Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250|UniProtKB:P04746};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; X99729; CAA68065.1; -; mRNA.
DR   AlphaFoldDB; P91778; -.
DR   SMR; P91778; -.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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; 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   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Carbohydrate metabolism; Chloride; Disulfide bond; Glycosidase;
KW   Hydrolase; Metal-binding; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..508
FT                   /note="Alpha-amylase"
FT                   /id="PRO_0000001396"
FT   ACT_SITE        212
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   ACT_SITE        248
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         116
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         173
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         182
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         210
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         216
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         311
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         349
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   SITE            313
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   DISULFID        46..102
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   DISULFID        156..175
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   DISULFID        383..389
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   DISULFID        455..467
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
SQ   SEQUENCE   508 AA;  56354 MW;  8824405C3949B465 CRC64;
     MLSLIIAACC VTVALAGTFS NPTCAPGRNT IVHLFEWKWT DIAKECERFL GPNGFCGVQI
     SPPNENRLVN NRPWWERYQP VSYKLQTRSG SEDQLRDMIS RCNRVNVRIY SDTVINHMTG
     VGGSGTGTAG SHWNGDTLSY PGVPFSAWDF NTGNECHSSD MNIHDYNNAE EIRNCRLVSL
     ADLKLSKNYV REEITQYMNH LIDLGVAGFR IDAAKHMWPG DLRAMFGTLH DLNSAVFGSG
     RKPFIFQEVI DMGGEPISAS EYTGIGRVTN FIFGVKLGQV FRNENKASNL HNWGEAWGMP
     NSNDVVVFID NHDNQRGHGG GGGPLTHFEP RPYKLATAFM LAHPYGFTRL MSSYNFDRSN
     TDQGPPHNGD NINDVTINAD LTCGNGWTCE HRWREIYNMV AFRNIVMGQN LQHWWDNGNY
     QIAFGRGNKG FIAMNMDNHN LDQTLQTGLP AGTYCDVISG SYDGSSCSGT EIQVGNDGNA
     HFSISNSSDD PMIAIHVGAK KGQPKVTT