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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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