ID AMYR_DROSU Reviewed; 494 AA.
AC O18420;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 22-FEB-2023, entry version 108.
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 subobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7241;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Montgenevre;
RX PubMed=9618501; DOI=10.1073/pnas.95.12.6848;
RA Da Lage J.-L., Renard E., Chartois F., Lemeunier F., Cariou M.-L.;
RT "Amyrel, a paralogous gene of the amylase gene family in Drosophila
RT melanogaster and the Sophophora subgenus.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:6848-6853(1998).
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; U79724; AAC48344.1; -; Genomic_DNA.
DR AlphaFoldDB; O18420; -.
DR SMR; O18420; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR FlyBase; FBgn0020466; Dsub\Amyrel.
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.
DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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 PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
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; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 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..20
FT /evidence="ECO:0000250"
FT CHAIN 21..494
FT /note="Alpha-amylase-related protein"
FT /id="PRO_0000001389"
FT ACT_SITE 208
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT ACT_SITE 245
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 206
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 308
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 343
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT SITE 310
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT MOD_RES 21
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT DISULFID 48..104
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 157..171
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 376..382
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 418..441
FT /evidence="ECO:0000255"
FT DISULFID 448..460
FT /evidence="ECO:0000250|UniProtKB:P56634"
SQ SEQUENCE 494 AA; 55602 MW; AFB4145BF8DE6DE9 CRC64;
MFKFTFALAL CVLAAGSALA QHNPHWWGNR NTIVHLFEWQ WEDIAEECEN FLGPRGFAGV
QVSPANENIV SPGRPWWERY QPISYKLITR SGDEEQFADM VRRCNDVGVR IYVDVLLNHM
SADFYGQAVG TAGTEADPAT KSFPGVPYTA EDFHPSCQIY DWNDRFQIQQ CELVGLKDLD
QSRDHVRTKL IEFLDHLIEL GVAGFRVDAA KHMASEDLEF IYGSLSDLKT EHGFPHNARP
FIFQEVIDHG GQEVTREEYN SLGAVTEFRF WQEIGNAFRG NNAFKWLQSW GTDWGFFSSG
QAFTFVDNHD NQRDGGAVLT YKIPRQYKMA TAFHLAYPYG ISRVMSSFAF DDHDSAPPQN
AQEQLISPEF DSDGACVNGW ICEHRWRQIY NMVGFKNAVR DTPVTNWWDN GDSQIAFCRG
SKGFIAINNN LYDLAETLQT CLPAGVYCDV ISGDLIHGSC SGKSVTVGND GRAFVSIGSN
DFDGVLAIHV DAKL
//
