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Database: UniProt
Entry: A0A0M4EDA9_DROBS
LinkDB: A0A0M4EDA9_DROBS
Original site: A0A0M4EDA9_DROBS 
ID   A0A0M4EDA9_DROBS        Unreviewed;       490 AA.
AC   A0A0M4EDA9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=alpha-glucosidase {ECO:0000256|ARBA:ARBA00012741};
DE            EC=3.2.1.20 {ECO:0000256|ARBA:ARBA00012741};
GN   ORFNames=Dbus_chr2Rg505 {ECO:0000313|EMBL:ALC40926.1};
OS   Drosophila busckii (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC40926.1, ECO:0000313|Proteomes:UP000494163};
RN   [1] {ECO:0000313|EMBL:ALC40926.1, ECO:0000313|Proteomes:UP000494163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole larvae {ECO:0000313|EMBL:ALC40926.1};
RA   Zhou Q., Bachtrog D.;
RT   "Ancestral chromatin configuration constrains chromatin evolution on
RT   differentiating sex chromosomes in Drosophila.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-
CC         glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC         Evidence={ECO:0000256|ARBA:ARBA00001657};
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DR   EMBL; CP012524; ALC40926.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M4EDA9; -.
DR   SMR; A0A0M4EDA9; -.
DR   STRING; 30019.A0A0M4EDA9; -.
DR   OMA; LMYEWRD; -.
DR   Proteomes; UP000494163; Chromosome 2r sequence.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11328; AmyAc_maltase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045857; O16G_dom_2.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF236; ALPHA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000494163};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          24..409
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   490 AA;  55922 MW;  E0E7454231C6A4C1 CRC64;
     MLGVASAKTA TPEIDWWENA ALYQIYPRSF QDSNDDGVGD LNGITQRLGY LKEIGITATW
     LSPIFTSPMA DFGYDISNFT EIDPSFGTLD DFDAMLAHAK SLGIKIILDF VPNHSSDECD
     WFKKSVAREP GYEDFYVWHV GKHNPETNQQ EPPSNWISVF GGSQWTWVHE RGEFYLHQFQ
     RKQPDLNFNN PLVRERMLEV LRFWLDRGVD GFRIDAVPHM YERQNADGSY PDEPISGWGS
     NASAYDYHDH IYTKDQPATV QLMYEWRDFL LQYQAEHGGA TRVLLAEAYS PVETLSAYFG
     NGQRQGTQLP MNFQLMYLNG YSNARQVVDS IDYWMNTMWA QHQTANWVVG NHDTPRVADR
     MGAHKVDLLN VIVNALPGAS VTYYGEEIGM SNVQTPCTEI SCDARDGERT PMQWSPLRHA
     DFSTAPSTWL PLSPDYQRFN VKTERGVARS SLQVFKAMQQ LKRSAAFMAF KQPGGFSYKA
     LTEQVLQIVR
//
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