ID   MAL1_APIME              Reviewed;         567 AA.
AC   Q17058;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Alpha-glucosidase;
DE            EC=3.2.1.20;
DE   AltName: Full=Maltase;
DE   Flags: Precursor;
OS   Apis mellifera (Honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Apis.
OX   NCBI_TaxID=7460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 18-41; 116-137 AND
RP   255-267.
RC   TISSUE=Hypopharyngeal gland;
RX   PubMed=8619864; DOI=10.1006/bbrc.1996.0604;
RA   Ohashi K., Sawata M., Takeuchi H., Natori S., Kubo T.;
RT   "Molecular cloning of cDNA and analysis of expression of the gene for
RT   alpha-glucosidase from the hypopharyngeal gland of the honeybee apis
RT   mellifera L.";
RL   Biochem. Biophys. Res. Commun. 221:380-385(1996).
RN   [2]
RP   CHARACTERIZATION.
RC   TISSUE=Hypopharyngeal gland;
RX   PubMed=8882720; DOI=10.1093/oxfordjournals.jbchem.a021237;
RA   Kubo T., Sasaki M., Nakamura J., Sasagawa H., Ohashi K., Takeuchi H.,
RA   Natori S.;
RT   "Change in the expression of hypopharyngeal-gland proteins of the worker
RT   honeybees (Apis mellifera L.) with age and/or role.";
RL   J. Biochem. 119:291-295(1996).
CC   -!- FUNCTION: Converts sucrose in nectar to glucose and fructose.
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   -!- SUBUNIT: Monomer.
CC   -!- TISSUE SPECIFICITY: Expressed specifically in the hypopharyngeal glands
CC       of the forager (worker) honeybee.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; D79208; BAA11466.1; -; mRNA.
DR   PIR; JC4714; JC4714.
DR   RefSeq; NP_001011608.1; NM_001011608.1.
DR   RefSeq; XP_006560868.1; XM_006560805.2.
DR   RefSeq; XP_006560869.1; XM_006560806.2.
DR   RefSeq; XP_006560870.1; XM_006560807.2.
DR   RefSeq; XP_016767968.1; XM_016912479.1.
DR   RefSeq; XP_016767969.1; XM_016912480.1.
DR   RefSeq; XP_016767971.1; XM_016912482.1.
DR   AlphaFoldDB; Q17058; -.
DR   SMR; Q17058; -.
DR   STRING; 7460.Q17058; -.
DR   BindingDB; Q17058; -.
DR   ChEMBL; CHEMBL4406; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PaxDb; 7460-GB43247-PA; -.
DR   EnsemblMetazoa; NM_001011608; NP_001011608; GeneID_406131.
DR   GeneID; 406131; -.
DR   KEGG; ame:406131; -.
DR   CTD; 406131; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   InParanoid; Q17058; -.
DR   OrthoDB; 3680211at2759; -.
DR   PhylomeDB; Q17058; -.
DR   SABIO-RK; Q17058; -.
DR   PRO; PR:Q17058; -.
DR   Proteomes; UP000005203; Linkage group LG6.
DR   Proteomes; UP001105180; Linkage Group LG6.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
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:SF233; MALTASE A1; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:8619864"
FT   CHAIN           18..567
FT                   /note="Alpha-glucosidase"
FT                   /id="PRO_0000001452"
FT   ACT_SITE        223
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        286
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            348
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        290
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        313
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        319
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        499
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        507
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   567 AA;  65565 MW;  A14D88DD657C99C2 CRC64;
     MKAVIVFCLM ALSIVDAAWK PLPENLKEDL IVYQVYPRSF KDSNGDGIGD IEGIKEKLDH
     FLEMGVDMFW LSPIYPSPMV DFGYDISNYT DVHPIFGTIS DLDNLVSAAH EKGLKIILDF
     VPNHTSDQHE WFQLSLKNIE PYNNYYIWHP GKIVNGKRVP PTNWVGVFGG SAWSWREERQ
     AYYLHQFAPE QPDLNYYNPV VLDDMQNVLR FWLRRGFDGF RVDALPYICE DMRFLDEPLS
     GETNDPNKTE YTLKIYTHDI PETYNVVRKF RDVLDEFPQP KHMLIEAYTN LSMTMKYYDY
     GADFPFNFAF IKNVSRDSNS SDFKKLVDNW MTYMPPSGIP NWVPGNHDQL RLVSRFGEEK
     ARMITTMSLL LPGVAVNYYG DEIGMSDTYI SWEDTQDPQG CGAGKENYQT MSRDPARTPF
     QWDDSVSAGF SSSSNTWLRV NENYKTVNLA AEKKDKNSFF NMFKKFASLK KSPYFKEANL
     NTRMLNDNVF AFSRETEDNG SLYAILNFSN EEQIVDLKAF NNVPKKLNMF YNNFNSDIKS
     ISNNEQVKVS ALGFFILISQ DAKFGNF
//