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
//
