AMYR_DROWI
ID AMYR_DROWI Reviewed; 492 AA.
AC O76263;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
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 willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Da Lage J.-L.;
RL Submitted (DEC-1997) 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; AF039560; AAC39095.1; -; Genomic_DNA.
DR AlphaFoldDB; O76263; -.
DR SMR; O76263; -.
DR STRING; 7260.FBpp0239873; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR eggNOG; KOG2212; Eukaryota.
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..18
FT /evidence="ECO:0000250"
FT CHAIN 19..492
FT /note="Alpha-amylase-related protein"
FT /id="PRO_0000001393"
FT ACT_SITE 206
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT ACT_SITE 243
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:P56634"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 204
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 306
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 341
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT SITE 308
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT MOD_RES 19
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT DISULFID 46..102
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 155..169
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 374..380
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 416..439
FT /evidence="ECO:0000255"
FT DISULFID 446..458
FT /evidence="ECO:0000250|UniProtKB:P56634"
SQ SEQUENCE 492 AA; 55641 MW; DFC711A762D8715D CRC64;
MRLSLSVLLC LGLALTLAQH NPHWWGNRNT IVHLFEWKWT DIADKCERFL GPRGYAGVQV
SPANENIISE GRPWWERYQP ISYKLVTRSG NELEFASMVK RCNDVGVRIY VDVLLNHMSA
DFEGLATGTG GSVAEPAKKS FPSVPYTADD FHETCEITDW NDRFQVQQCE LVGLKDLNQN
RDWVRTKLIE FLDHLIELGV AGFRVDAAKH MASEDLSFIY SSVRDLNINH GFPNNARPFI
YQEVIDHGHE TVTREEYNEL GAVTEFRFSE EIGKAFRGNN ALKWLQSWGT DWGFLSSGQA
LTFVDNHDNQ RDSGDVLNYK SPKQYKMATA FHLAYPYGIS RVMSSFGFDD RDQAPPQDAQ
EQLISPEFDA DGGCTNGWIC EHRWRQIYNM VEFKNTVRDT ELTNWWDNGD NQIAFCRGSK
GFIAINNNLY NLSETLQTCL PAGEYCDVIS GSLVDGACTG KSVSVDGNGY GYIHIGTEDF
DGVLAIHTDA KL
