ID   AGLU_HORVU              Reviewed;         877 AA.
AC   Q43763;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Alpha-glucosidase;
DE            EC=3.2.1.20;
DE   AltName: Full=Maltase;
DE   Flags: Precursor;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Morex; TISSUE=Aleurone;
RX   PubMed=8616248; DOI=10.1007/bf00020110;
RA   Tibbot B.K., Skadsen R.W.;
RT   "Molecular cloning and characterization of a gibberellin-inducible,
RT   putative alpha-glucosidase gene from barley.";
RL   Plant Mol. Biol. 30:229-241(1996).
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   -!- TISSUE SPECIFICITY: High levels seen in the aleurone and scutellum
CC       after germination, while low levels are found in developing seeds.
CC   -!- DEVELOPMENTAL STAGE: Levels increase steadily throughout imbibition
CC       reaching maximum levels at day 7. During germination, levels increase
CC       from day 2, reach maximum levels at day 3 and decline after day 5.
CC   -!- INDUCTION: By gibberellin A3 (GA).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR   EMBL; U22450; AAB02985.1; -; mRNA.
DR   PIR; S65057; S65057.
DR   AlphaFoldDB; Q43763; -.
DR   SMR; Q43763; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   BRENDA; 3.2.1.20; 2687.
DR   ExpressionAtlas; Q43763; baseline and differential.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044275; P:cellular carbohydrate catabolic process; IEA:UniProt.
DR   Gene3D; 2.60.40.1180; -; 2.
DR   InterPro; IPR031727; Gal_mutarotase_N.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR000322; Glyco_hydro_31.
DR   InterPro; IPR030458; Glyco_hydro_31_AS.
DR   InterPro; IPR030459; Glyco_hydro_31_CS.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF13802; Gal_mutarotas_2; 1.
DR   Pfam; PF01055; Glyco_hydro_31; 1.
DR   Pfam; PF16863; NtCtMGAM_N; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
DR   PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR   PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..877
FT                   /note="Alpha-glucosidase"
FT                   /id="PRO_0000018583"
FT   REGION          89..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        437
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        440
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        534
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        298
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        391
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        471
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        570
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   877 AA;  96933 MW;  E3B5C16E4588C492 CRC64;
     MATVGVLLLC LCLCLFAPRL CSSKEEGPLA ARTVLAVAVT MEGALRAEAA TGGRSSTGDV
     QRLAVYASLE TDSRLRVRIT DADHPRWEVP QDIIPRPAPG DVLHDAPPAS SAPLQGRVLS
     PAGSDLVLTV HASPFRFTVS RRSTGDTLFD TAPGLVFRDK YLEVTSALPA GRASLYGLGE
     HTKSSFRLRH NDSFTLWNAD IGASYVDVNL YGSHPFYMDV RAPGTAHGVL LLSSNGMDVL
     YGGSYVTYKV IGGVLDFYFF AGPNPLAVVD QYTQLIARPA PMPYWSFGFH QCRYGYLNVS
     DLERVVARYA KARIPLEVMW TDIDYMDGFK DFTLDRVNFT AAELRPFVDR LHRNAQKYVL
     ILDPGIRVDP IDATYGTFVR GMQQDIFLKR NGTNFVGNVW PGDVYFPDFM HPAAAEFWAR
     EISLFRRTIP VDGLWIDMNE ISNFYNPEPM NALDDPPYRI NNDGTGRPIN NKTVRPLAVH
     YGGVTEYEEH NLFGLLEARA TGRGVLRDTG RRPFVLSRST FVGSGRYTAY WTGDNAATWG
     DLRYSINTML SFGLFGMPMI GADICGFNGN TTEELCGRWI QLGAFYPFSR DHSAIFTVRR
     ELYLWPSVAA SGRKALGLRY QLLPYFYTLM YEAHMTGAPI ARPLFFSYPH DVATYGVDRQ
     FLLGRGVLVS PVLEPGPTTV DAYFPAGRWY RLYDYSLAVA TRTGKHVRLP APADTVNVHL
     TGGTILPLQQ SALTTSRARR TAFHLLVALA EDGTASGYLF LDDGDSPEYG RRSDWSMVRF
     NYKIPNNKGA IKVKSEVVHN SYAQSRTLVI SKVVLMGHRS PAAPKKLTVH VNSAEVEASS
     SAGTRYQNAG GLGGVAHIGG LSLVVGEEFE LKVAMSY