AGLU_SPIOL
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 03-AUG-2022, entry version 86.
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 PRIDE; O04893; -.
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..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