AMYR_DROSI
ID AMYR_DROSI Reviewed; 493 AA.
AC O77016; O77017;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 3.
DT 03-AUG-2022, entry version 109.
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 simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CLONES SIM1/SIM92 AND SIM2).
RA Da Lage J.-L.;
RL Submitted (OCT-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U96159; AAC39109.4; -; Genomic_DNA.
DR EMBL; U96160; AAC39110.2; -; Genomic_DNA.
DR AlphaFoldDB; O77016; -.
DR SMR; O77016; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:EnsemblMetazoa.
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..19
FT /evidence="ECO:0000250"
FT CHAIN 20..493
FT /note="Alpha-amylase-related protein"
FT /id="PRO_0000001387"
FT ACT_SITE 207
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT ACT_SITE 244
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 205
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 307
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 342
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT SITE 309
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT DISULFID 47..103
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 156..170
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 375..381
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 417..440
FT /evidence="ECO:0000255"
FT DISULFID 447..459
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT VARIANT 50
FT /note="F -> L (in strain: Isolate SIM2)"
FT VARIANT 324
FT /note="K -> R (in strain: Isolate SIM2)"
SQ SEQUENCE 493 AA; 55551 MW; 388EA33DFBDFCDEE CRC64;
MFKFALTLTL CLAGSLSLAQ HNPHWWGNRN TIVHLFEWKW SDIAQECESF LGPRGFAGVQ
VSPVNENIIS AGRPWWERYQ PISYKLTTRS GNEEEFGDMV RRCNDVGVRI YVDVLLNHMS
GDFDGVAVGT AGTEAEPRKK SFPGVPYTAQ DFHPTCEITD WNDRFQVQQC ELVGLKDLDQ
SSDWVRSKLI EFLDHLIELG VAGFRVDAAK HMASEDLEYI YSSLSNLNID HGFPHNSRPF
IFQEVIDHGH ETVSRDEYKE LGAVTEFRFS EEIGNAFRGN NALKWLQSWG TGWGFLPSGQ
ALTFVDNHDN QRDAGAVLNY KSPKQYKMAT AFHLAYPYGI SRVMSSFAFD DHDTPPPQDA
QERIISPEFD EDGACVNGWI CEHRWRQIYA MVGFKNAVRD TEITGWWDNG DNQISFCRGN
KGFLAINNNQ YDLSQDLNTC LPTGTYCDVI SGSLIDGSCT GKSVTVNENG YGYIHIGSDD
FDGVLALHVD AKV
