AMY_TRICA
ID AMY_TRICA Reviewed; 489 AA.
AC P09107;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 120.
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; Fragment;
OS Tribolium castaneum (Red flour beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX NCBI_TaxID=7070;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3129570; DOI=10.1007/bf02099856;
RA Hickey D.A., Benkel B.F., Boer P.H., Genest Y., Abukashawa S.,
RA Ben-David G.;
RT "Enzyme-coding genes as molecular clocks: the molecular evolution of animal
RT alpha-amylases.";
RL J. Mol. Evol. 26:252-256(1987).
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; X06905; CAA30009.1; -; Genomic_DNA.
DR PIR; A29347; A29347.
DR AlphaFoldDB; P09107; -.
DR SMR; P09107; -.
DR STRING; 7070.TC000937-PA; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; P09107; -.
DR eggNOG; KOG2212; Eukaryota.
DR HOGENOM; CLU_013336_2_1_1; -.
DR BRENDA; 3.2.1.1; 6437.
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; Signal.
FT SIGNAL <1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..489
FT /note="Alpha-amylase"
FT /id="PRO_0000001395"
FT ACT_SITE 203
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT ACT_SITE 240
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 164
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 201
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 303
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 339
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT SITE 305
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 44..102
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 152..166
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 372..378
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 443..455
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT NON_TER 1
SQ SEQUENCE 489 AA; 53247 MW; D1AB107C48FF8721 CRC64;
HFKPILVLCL ATLALGLFVP HFAADRNSIV HLFEWKWSDI ADECERFLAP KGFGGVQISP
PNENLVVTSS NRPWWERYQP VSYILNTRSG DEAALADMIS RCNAVGVRIY VDTVINHMTG
MGGTGTAGSQ ADRDGKNYPA VPYGSGDFHD SCTVNNYQDA SNVRNCELVG LADLNQGSDY
VRSKIIEYMN HLVDLGVAGF RVDAAKHMWP ADLEAIYASL KNLNTDHGFL DGQKPFIFQE
VIDLGGEAIS KHEYTGFGTV IEFQYGLSLG NAFQGGNQLA NLANWGPEWN LLDGLDAVAF
IDNHDNQRTG GSQILTYKNP KPYKMAIAFM LAHPYGTTRL MSSFAFDNND QGPPQDDAGN
LISPSINDDG TCGNGYVCEH RWRQIFNMVG FRNAVQGTGI ENWWSDGNQQ IAFGRGNKGF
VAFTIGYDLN QHLQTGLPAG SYCDVISGNA ENGSCSGKTI TVGGDGYADI SLGANEDDGV
IAIHVNAKL
