ID   AGALB_TALEM             Reviewed;         452 AA.
AC   A7XZT2;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Probable alpha-galactosidase B;
DE            EC=3.2.1.22;
DE   AltName: Full=Melibiase B;
DE   Flags: Precursor;
OS   Talaromyces emersonii (Thermophilic fungus) (Rasamsonia emersonii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX   NCBI_TaxID=68825;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Murray P.G., Gernig A., Simila J., Fernandes S.L., Tuohy M.G.;
RL   Submitted (AUG-2007) 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; EU106878; ABU94728.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7XZT2; -.
DR   SMR; A7XZT2; -.
DR   CAZy; GH27; Glycoside Hydrolase Family 27.
DR   CLAE; MEL27A_RASEM; -.
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   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..452
FT                   /note="Probable alpha-galactosidase B"
FT                   /id="PRO_0000393222"
FT   ACT_SITE        157
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        253
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         231..235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        292
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        391
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        409
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        410
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        47..79
FT                   /evidence="ECO:0000250"
FT   DISULFID        129..159
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   452 AA;  49352 MW;  250FC613FAB762CC CRC64;
     MLHRATTTAA AAAAAALLLC PVQALVRPDG VGKLPALGWN SWNAFGCDID EEKILTAANQ
     IVNLGLKDLG YEYVNIDDCW SVKSGRNATT GRIMPDLTKF PDGISGLAEK IHNLGLKIGI
     YSSAGWTTCA GYPASLGNET IDAETFAEWG IDYLKYDNCG VPPDWQDQYS YCVPDSGDPA
     TNPNGTCPNL QNPAPAVYDW RTSKTAERYR RMRDALLGVQ DKRTILFSLC DWGQADVNEW
     GAETGNSWRM SGDISPNWPR ISTIANLNSF ELNSVDFWGH NDPDMLEVGN GNLTLAENRA
     HFALWAAMKS PLIIGTALDK IDQDHLSILS NKYLLTFHQD PQIGRPAYPY KWGYNPDWTF
     DPGHPAEYWS GPTSSGDVLV LMLNTESGPA NRTAVWSEVP ELKGRNNNNN SSSTGFQVTD
     AWTGSSLGCV QGGYSVELES HDVAVLVVSG EC