ID   AMYR_DROBA              Reviewed;         494 AA.
AC   O77019;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Alpha-amylase-related protein;
DE            EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
DE   Flags: Precursor;
GN   Name=Amyrel;
OS   Drosophila bakoue (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=30018;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Da Lage J.-L.;
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
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:P56634};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P56634};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000250|UniProtKB:P56634};
CC       Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250|UniProtKB:P56634};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; U96162; AAC39112.2; -; Genomic_DNA.
DR   AlphaFoldDB; O77019; -.
DR   SMR; O77019; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   FlyBase; FBgn0021666; Dbak\Amyrel.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   Calcium; Carbohydrate metabolism; Chloride; Disulfide bond; Glycosidase;
KW   Hydrolase; Metal-binding; Pyrrolidone carboxylic acid; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..494
FT                   /note="Alpha-amylase-related protein"
FT                   /id="PRO_0000001371"
FT   ACT_SITE        208
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   ACT_SITE        245
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         118
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   BINDING         169
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   BINDING         178
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   BINDING         206
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   BINDING         212
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   BINDING         308
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   BINDING         343
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   SITE            310
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   MOD_RES         21
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   DISULFID        48..104
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   DISULFID        157..171
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   DISULFID        376..382
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   DISULFID        418..441
FT                   /evidence="ECO:0000255"
FT   DISULFID        448..460
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
SQ   SEQUENCE   494 AA;  55666 MW;  0D45A4327B761299 CRC64;
     MIKFALALTL CLAGASLSLA QHNPRWWGNR NTIVHLFEWK WSDIAEECET FLAPRGFAGV
     QVSPVNENII SAGRPWWERY QPISYKLTTR SGNEEEFADM VRRCNDVGIR IYVDVLLNHM
     SGDFDGVAVG TAGTEAEPSK KSFPGVPYTA QDFHPSCEIT DWNNRFQVQE CELVGLKDLN
     QHSDYVRSKL IEFLDHLIEL GVAGFRVDAA KHMAAVDLEY IYGSLSNLNI EHGFPHNARP
     FIFQEVIDHG HETVSREEYN ELGAVTEFRF SEEIGKAFRG NNALKWLQSW GTDWGFLNSD
     QALTFVDNHD NQRDQGSVLN YKSPRQYKMA TAFHLAYPYG ISRVMSSFAF DDHDTPPPQD
     AQENIISPEF DEDGACVNGW ICEHRWRQIY AMVGFKNAVR DTELSGWWDN GDNQISFCRG
     NKGFLAVNNN LYDLSQELNT CLPAGEYCDV ISGSLVDGAC TGKSVTVNEH GYGYIHIGSD
     DFDGVLALHV NAKV