AMYA_DROMA
ID AMYA_DROMA Reviewed; 494 AA.
AC P54215;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Alpha-amylase A;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE Flags: Precursor;
GN Name=Amy-d;
GN and
GN Name=Amy-p;
OS Drosophila mauritiana (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8536970; DOI=10.1093/genetics/141.1.223;
RA Shibata H., Yamazaki T.;
RT "Molecular evolution of the duplicated Amy locus in the Drosophila
RT melanogaster species subgroup: concerted evolution only in the coding
RT region and an excess of nonsynonymous substitutions in speciation.";
RL Genetics 141:223-236(1995).
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; D17729; BAA04583.1; -; Genomic_DNA.
DR EMBL; D17730; BAA04584.1; -; Genomic_DNA.
DR PIR; S58939; S58939.
DR PIR; S58940; S58940.
DR AlphaFoldDB; P54215; -.
DR SMR; P54215; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR FlyBase; FBgn0012498; Dmau\Amy-d.
DR FlyBase; FBgn0012499; Dmau\Amy-p.
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; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..494
FT /note="Alpha-amylase A"
FT /id="PRO_0000001363"
FT ACT_SITE 204
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT ACT_SITE 241
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 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 202
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 304
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 343
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT SITE 306
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT MOD_RES 19
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 46..102
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 153..167
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 376..382
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 448..460
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT VARIANT 7
FT /note="L -> I (in Amy-P)"
FT VARIANT 398
FT /note="T -> A (in Amy-P)"
SQ SEQUENCE 494 AA; 53730 MW; F557075877241E56 CRC64;
MFLAKSLVCL ALLAVANAQF DTNYASGRSG MVHLFEWKWD DIAAECENFL GPNGFAGVQV
SPVNENAVKD SRPWWERYQP ISYKLETRSG NEQQFASMVK RCNAVGVRIY VDVIFNHMAA
DGGTYGTGGS TASPSSKSYP GVPYSSLDFN PTCAINNYND ANQVRNCELV GLRDLNQGNS
YVQDKVVEFL DHLIDLGVAG FRVDAAKHMW PADLAVIYGR LKNLNTDHGF ASGSKAYIVQ
EVIDMGGEAI SKSEYTGLGA ITEFRHSDSI GKVFRGKDQL QYLTNWGTAW GFAASDRSLV
FVDNHDNQRG HGAGGADVLT YKVPKQYKMA SAFMLAHPFG TPRVMSSFSF SDTDQGPPTT
DGHNIASPVF NSDNSCSGGW VCEHRWRQIY NMVAFRNTVG SDAIQNWWDN GSNQISFSRG
SRGFVAFNND NYDLNSSLQT GLPAGTYCDV ISGSKSGSSC TGKTVSVGSD GRASIYIGSS
EDDGVLAIHV NAKL
