ID   G1CH69_DROMA            Unreviewed;       493 AA.
AC   G1CH69;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   22-FEB-2023, entry version 39.
DE   RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE            EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN   Name=Amyrel {ECO:0000313|EMBL:AEK11628.1};
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 {ECO:0000313|EMBL:AEK11628.1};
RN   [1] {ECO:0000313|EMBL:AEK11628.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21599771; DOI=10.1111/j.1365-294X.2011.05127.x;
RA   Legrand D., Chenel T., Campagne C., Lachaise D., Cariou M.L.;
RT   "Inter-island divergence within Drosophila mauritiana, a species of the D.
RT   simulans complex: Past history and/or speciation in progress?";
RL   Mol. Ecol. 20:2787-2804(2011).
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:0000256|ARBA:ARBA00000548};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000256|ARBA:ARBA00001923};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; JF815729; AEK11628.1; -; Genomic_DNA.
DR   AlphaFoldDB; G1CH69; -.
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:InterPro.
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 {ECO:0000256|ARBA:ARBA00022837};
KW   Chloride {ECO:0000256|ARBA:ARBA00023214};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..493
FT                   /note="alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003412017"
FT   DOMAIN          30..395
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          404..492
FT                   /note="Alpha-amylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00632"
SQ   SEQUENCE   493 AA;  55524 MW;  4FF18F3C627D37A8 CRC64;
     MFKFALTLTL CLAGSLSLAQ HNPHWWGNRN TIVHLFEWKW SDIAQECESF LGPRGFAGVQ
     VSPVNENIIA AGRPWWERYQ PISYKLTTRS GNEEEFGDMV RRCNDVGVRI YVDVLLNHMS
     GDFDGVAVGT AGTEAEPRKK SFPGVPYTAQ DFHPTCEITD WNDRFQVQQC ELVGLKDLDQ
     SSDWVRSKLI EFLDHLIELG VAGFRVDAAK HMASEDLEYI YSSLSNLNID HGFPHNSRPF
     IFQEVIDHGH ETVSRDEYKD LGAVTEFRFS EEIGNAFRGN NALKWLQSWG TGWGFLPSGQ
     ALTFVDNHDN QRDAGAVLNY KSPRQYKMAT AFHLAYPYGV SRVMSSFAFD DHDTPPPQDA
     QERIISPEFD EDGACVNGWI CEHRWRQIYA MVGFKNAVRD TEITGWWDNG DNQISFCRGN
     KGFLAFNNNL YDLSQDLNTC LPAGTYCDVI SGSLIDGSCT GKSVTVNENG YGYIHIGSDD
     FDGVLALHVD AKV
//