ID   AMY_TITSE               Reviewed;          38 AA.
AC   P85843;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Alpha-amylase;
DE            EC=3.2.1.1;
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE   Flags: Fragment;
OS   Tityus serrulatus (Brazilian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=6887;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Venom {ECO:0000269|Ref.1};
RA   Richardson M., Borges M.H., Cordeiro M.N., Pimenta A.M.C., de Lima M.E.,
RA   Rates B.;
RT   "Alpha-amylase from venom of Brazilian spider Tityus serrulatus.";
RL   Submitted (MAY-2008) to UniProtKB.
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   -!- 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|UniProtKB:P04746}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000255}.
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DR   AlphaFoldDB; P85843; -.
DR   SMR; P85843; -.
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.
PE   1: Evidence at protein level;
KW   Calcium; Carbohydrate metabolism; Chloride; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Metal-binding; Secreted.
FT   CHAIN           1..>38
FT                   /note="Alpha-amylase"
FT                   /id="PRO_0000343463"
FT   DISULFID        29..?
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   NON_TER         38
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   38 AA;  4619 MW;  69205C5718332BE1 CRC64;
     KYYEPNTVQG RSVIVHLFEW RWKDVADECE QFLSPKGY