ID   AGLU_SPIOL              Reviewed;         903 AA.
AC   O04893;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Alpha-glucosidase;
DE            EC=3.2.1.20;
DE   AltName: Full=Maltase;
DE   Flags: Precursor;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Dash;
RX   PubMed=9132069; DOI=10.1023/a:1005766003923;
RA   Sugimoto M., Furui S., Suzuki Y.;
RT   "Molecular cloning and characterization of a cDNA encoding alpha-
RT   glucosidase from spinach.";
RL   Plant Mol. Biol. 33:765-768(1997).
CC   -!- FUNCTION: Alpha-glucosidase I and II have high activity towards malto-
CC       oligosaccharides and starch, while form III and IV have high activity
CC       towards malto-oligosaccharides but low activity toward 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   -!- PTM: Four different forms (I-IV) may be produced by post-translational
CC       modification.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR   EMBL; D86624; BAA19924.1; -; mRNA.
DR   PIR; T09143; T09143.
DR   AlphaFoldDB; O04893; -.
DR   SMR; O04893; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   Proteomes; UP001155700; Unplaced.
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;
KW   Reference proteome; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..903
FT                   /note="Alpha-glucosidase"
FT                   /id="PRO_0000018584"
FT   ACT_SITE        465
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        468
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        564
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        400
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        491
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        501
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        600
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   903 AA;  100881 MW;  5B054E27C20EC33A CRC64;
     MKKKIPSLAL GILLVFLLQY LVAGISTSEN DPEGVIGYGY KVKSVKVDSG TRRSLTALPQ
     LVKNSSVYGP DIQLLSITAS LESNDRLRVR ITDAKHRRWE IPDNILHRHQ PPPPPPHSLS
     SLYRTLLSSP TTNRRKILLS HPNSDLTFSL INTTPFGFTI SRKSTHDVLF DATPDPTNPN
     TFLIFIDQYL HLTSSLPGTR AHIYGLGEHS KPTFQLAHNQ TLTMRAADIP SSNPDVNLYG
     SHPFYMDVRS SPVAGSTHGV LLLNSNGMDV EYTGNRITYK VIGGIIDLYF FAGPSPGQVV
     EQFTRVIGRP APMPYWAFGF QQCRYGYHDV YELQSVVAGY AKAKIPLEVM WTDIDYMDAY
     KDFTLDPVNF PLDKMKKFVN NLHKNGQKYV VILDPGISTN KTYETYIRGM KHDVFLKRNG
     KPYLGSVWPG PVYFPDFLKP SALTFWTDEI KRFLNLLPVD GLWIDMNEIS NFISSPPIPG
     STLDNPPYKI NNSGVMLPII NKTIPPTAMH YGDIPEYNVH NLFGYLEARV TRAALIKLTE
     KRPFVLSRST FSGSGKYTAH WTGDNAATWN DLVYSIPSML DFGLFGIPMV GADICGFLGN
     TTEELCRRWI QLGAFYPFSR DHSSLGTTYQ ELYRWESVAA SARKVLGLRY TLLPYFYTLM
     YEAQLNGIPI ARPLFFSFPD DIKTYGISSQ FLLGKGVMVS PVLKPGVVSV TAYFPRGNWF
     DLFDYTRSVT ASTGRYVTLS APPDHINVHI QEGNILAMQG KAMTTQAARK TPFHLLVVMS
     DCGASFGELF LDDGVEVTMG VNRGKWTFVK FIAASAKQTC IITSDVVSGE FAVSQKWVID
     KVTILGLRKG TKINGYTVRT GAVTRKGDKS KLKSTPDRKG EFIVAEISGL NLLLGREFKL
     VLH
//