ID   AGLU_MUCJA              Reviewed;         864 AA.
AC   Q92442;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Alpha-glucosidase;
DE            EC=3.2.1.20;
DE   AltName: Full=Maltase;
DE   Flags: Precursor;
OS   Mucor javanicus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=51122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=DSM 1222 / BCRC 31544 / NBRC 4570 / NRRL 13035;
RX   PubMed=8830045; DOI=10.1093/oxfordjournals.jbchem.a021269;
RA   Sugimoto M., Suzuki Y.;
RT   "Molecular cloning, sequencing, and expression of a cDNA encoding alpha-
RT   glucosidase from Mucor javanicus.";
RL   J. Biochem. 119:500-505(1996).
CC   -!- FUNCTION: Hydrolyzes not only malto-oligosaccharides but also soluble
CC       starch.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR   EMBL; D67034; BAA11053.1; -; mRNA.
DR   AlphaFoldDB; Q92442; -.
DR   SMR; Q92442; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   CLAE; AGL31A_MUCJA; -.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   CDD; cd06602; GH31_MGAM_SI_GAA; 1.
DR   CDD; cd14752; GH31_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR030458; Glyco_hydro_31_AS.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR030459; Glyco_hydro_31_CS.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR22762:SF133; ALPHA-GLUCOSIDASE; 1.
DR   Pfam; PF13802; Gal_mutarotas_2; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..864
FT                   /note="Alpha-glucosidase"
FT                   /id="PRO_0000018580"
FT   ACT_SITE        430
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10066"
FT   ACT_SITE        433
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        567
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        364
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        406
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        466
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        500
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        568
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        734
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   864 AA;  98761 MW;  CFAB4759DC431403 CRC64;
     MAKVSFIFVA IALITGNVLC QTDATYAVSS SAPGYKIDGH VRKTEAGLHI PLTLNSRGNK
     KTGIDTFGKT IKDITVDVEY ETEERLHVKI SDKAKKQYLV PDSPLGFERP QIKHYVSPKH
     SNLDFQYTAK PFSFKVVRKD DKTTIFDTTN MPLVFEDQYL ELSTKVPEDA NIYGIGEVTA
     PFRRTHNVTT LWARDNPDDF YRNIYGAHPY YQEVRDGKAH GALLMNAHGM DVITTEGRIT
     YKVIGGILDF YFFAPKSGKP NDLSIAYTDL IGKPMMPSHW MLGWHHCRYG YPNIDKVETV
     KRKYKEANIP LQTVWVDIDY MEETKDFTFD KVNFPQDRMI GLGEQLHKDG QNYVVMVDPA
     ISANTTYEPY VRGTEMDVWI KNADGSDFIG SVWPGFTTFP DWWHPNATKY WNKEIIDFVD
     MLGVDGLWID MNEPASFCLG SCGSGKVDAG NQPYRWTYTE EEQAANHTRW EKELKAMGNP
     PGEERNLLYP KYAINNGAGN LSEFTVATTA LHYGNIPHYD IHNLYGHAES HITRQALIKH
     KNKIRPFVLT RSSFPGSGKS VGHWTGDNHS FWPYLKNSIA NILNFQMFGV SYSGADVCGF
     NSDTTEELCT RWMEIGAFYP FARNHNNNAA KDQEPYLWES TAEASRIAIN TRYEMLPYFY
     TLFEESNRLG LGVWRPLIFE YPAYEELVSN DVQTLVGSDI LLSPVLDEGK TSVKAQFPGG
     QWYDWYTHEL TVDNKSNKKV KTVTLDAPLT HIPIHIRGGA IIPTKTPKYT VGETFATPYN
     LVIALDKKGQ ASGRLYIDDG ESLEVKSSSG YHFHLQEWSP QGFWQVWLQE GRKDWLHHHY
     WQARQQVAKG SRWQEDYQID PWQE
//