ID   AGLU_BETVU              Reviewed;         913 AA.
AC   O04931;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Alpha-glucosidase;
DE            EC=3.2.1.20;
DE   AltName: Full=Maltase;
DE   Flags: Precursor;
OS   Beta vulgaris (Sugar beet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX   NCBI_TaxID=161934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. NK-152;
RX   PubMed=9178565; DOI=10.1271/bbb.61.875;
RA   Matsui H., Iwanami S., Ito H., Mori H., Honma M., Chiba S.;
RT   "Cloning and sequencing of a cDNA encoding alpha-glucosidase from sugar
RT   beet.";
RL   Biosci. Biotechnol. Biochem. 61:875-880(1997).
RN   [2]
RP   ACTIVE SITE, AND PROTEIN SEQUENCE OF 464-472.
RX   PubMed=7766184; DOI=10.1271/bbb.59.459;
RA   Iwanami S., Matsui H., Kimura A., Ito H., Mori H., Honma M., Chiba S.;
RT   "Chemical modification and amino acid sequence of active site in sugar beet
RT   alpha-glucosidase.";
RL   Biosci. Biotechnol. Biochem. 59:459-463(1995).
CC   -!- FUNCTION: High activity for alpha-glucan.
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   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR   EMBL; D89615; BAA20343.1; -; mRNA.
DR   PIR; JC5463; JC5463.
DR   AlphaFoldDB; O04931; -.
DR   SMR; O04931; -.
DR   ChEMBL; CHEMBL4348; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   GO; GO:0004558; F:alpha-1,4-glucosidase activity; IMP:UniProtKB.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..913
FT                   /note="Alpha-glucosidase"
FT                   /id="PRO_0000018582"
FT   REGION          106..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..128
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        469
FT                   /evidence="ECO:0000269|PubMed:7766184"
FT   ACT_SITE        472
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        568
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        404
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        495
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        517
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        728
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        823
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   913 AA;  102117 MW;  02AC4F0B505369CC CRC64;
     MERSKLPRYI CPTLAVVLPL VLCMVVEGAT TSKNDNQGEA IGYGYQVKNA KVDNSTGKSL
     TALLQLIRNS PVYGPDIHFL SFTASFEEDD TLRIRFTDAN NRRWEIPNEV LPRPPPPPSP
     PPLSSLQHLP KPIPQNQPTT TVLSHPHSDL AFTLFHTTPF GFTIYRKSTH DVLFDATPIP
     SNPTTFLIYK DQYLQLSSSL PAQQAHLYGL GEHTKPTFQL AHNQILTLWN ADIASFNRDL
     NLYGSHPFYM DVRSSPMVGS THGVFLLNSN GMDVEYTGDR ITYKVIGGII DLYIFAGRTP
     EMVLDQYTKL IGRPAPMPYW AFGFHQCRWG YRDVNEIETV VDKYAEARIP LEVMWTDIDY
     MDAFKDFTLD PVHFPLDKMQ QFVTKLHRNG QRYVPILDPG INTNKSYGTF IRGMQSNVFI
     KRNGNPYLGS VWPGPVYYPD FLDPAARSFW VDEIKRFRDI LPIDGIWIDM NEASNFITSA
     PTPGSTLDNP PYKINNSGGR VPINSKTIPA TAMHYGNVTE YNAHNLYGFL ESQATREALV
     RPATRGPFLL SRSTFAGSGK YTAHWTGDNA ARWDDLQYSI PTMLNFGLFG MPMIGADICG
     FAESTTEELC CRWIQLGAFY PFSRDHSARD TTHQELYLWE SVAASARTVL GLRYELLPYY
     YTLMYDANLR GSPIARPLSF TFPDDVATYG ISSQFLIGRG IMVSPVLQPG SSIVNAYSPR
     GNWVSLSNYT SSVSVSAGTY VSLSAPPDHI NVHIHEGNIV AMQGEAMTTQ AARSTPFHLL
     VVMSDHVAST GELFLDNGIE MDIGGPGGKW TLVRFFAESG INNLTISSEV VNRGYAMSQR
     WVMDKITILG LKRRVKIKEY TVQKDAGAIK VKGLGRRTSS HNQGGFFVSV ISDLRQLVGQ
     AFKLELEFEG ATR