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 22-FEB-2023, entry version 98.
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 CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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 PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
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; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 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
//
