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AGALB_PENSI
ID   AGALB_PENSI             Reviewed;         435 AA.
AC   O94221;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Probable alpha-galactosidase B;
DE            EC=3.2.1.22;
DE   AltName: Full=Melibiase B;
DE   Flags: Precursor;
GN   Name=agl1;
OS   Penicillium simplicissimum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=69488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Luonteri E., Alatalo E., Siika-aho M., Tenkanen M., Penttilae M.;
RT   "Alpha-galactosidases of Penicillium simplicissimum; production,
RT   purification and characterisation of the gene encoding AGLI.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolyzes a variety of simple alpha-D-galactoside as well as
CC       more complex molecules such as oligosaccharides and polysaccharides.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC         residues in alpha-D-galactosides, including galactose
CC         oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
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DR   EMBL; AJ009956; CAA08915.1; -; mRNA.
DR   AlphaFoldDB; O94221; -.
DR   SMR; O94221; -.
DR   CAZy; GH27; Glycoside Hydrolase Family 27.
DR   CLAE; MEL27A_PENSI; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd14792; GH27; 1.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002241; Glyco_hydro_27.
DR   InterPro; IPR000111; Glyco_hydro_27/36_CS.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR041233; Melibiase_C.
DR   PANTHER; PTHR11452; PTHR11452; 1.
DR   Pfam; PF16499; Melibiase_2; 2.
DR   Pfam; PF17801; Melibiase_C; 1.
DR   PRINTS; PR00740; GLHYDRLASE27.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..435
FT                   /note="Probable alpha-galactosidase B"
FT                   /id="PRO_5000064513"
FT   ACT_SITE        151
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        243
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         221..225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        232
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        378
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        41..73
FT                   /evidence="ECO:0000250"
FT   DISULFID        123..153
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   435 AA;  47630 MW;  0B981E28EB8EB283 CRC64;
     MLTSLSLTAL ALLPSANALV RKDGVGRLPA LGWNSWNAFG CDVDSTKIMT AANEMVHLGL
     KDLGYEYVNI DDCWSVKNTR NSTTQRIIPD TQKFPDGISG VADQVHQLGL KIGIYSSAGE
     TTCAGYPASL GYEKVDAEAF AEWGIDYLKY DNCGVPSNWT DQYSSCVPDG SNEPANGTCP
     GLSNPAPAGY DWTKSNTFTR YTMMRDALLG QTRTILYSLC DWGQADVNTW GNETGNSWRM
     SGDISANWAR IAQIANENTF RMNYVGFWGH PDPDMLEVGN GDLTAAENRA HFALWAIMKS
     PLIIGTALDG ISDANLAVLK NKYLIEFNQD PIIGRSAHPY KWGYNPDWTF DPAHPAEYWS
     GPSSTLKGTL VLMLNSENST STRTAVWKEI PELKGHNAYR VTDAWSGKDL GCVKKQYSAS
     LASHDVAVLV VKEAC
 
 
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