ID   AGALB_ASPNG             Reviewed;         443 AA.
AC   Q9Y865;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Probable alpha-galactosidase B;
DE            EC=3.2.1.22;
DE   AltName: Full=Melibiase B;
DE   Flags: Precursor;
GN   Name=aglB;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX   PubMed=10347026; DOI=10.1128/aem.65.6.2453-2460.1999;
RA   de Vries R.P., van den Broeck H.C., Dekkers E., Manzanares P.,
RA   de Graaff L.H., Visser J.;
RT   "Differential expression of three alpha-galactosidase genes and a single
RT   beta-galactosidase gene from Aspergillus niger.";
RL   Appl. Environ. Microbiol. 65:2453-2460(1999).
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   -!- INDUCTION: Expression on xylan is very high, whereas elevated
CC       expression levels are also detected on galactose and xylose.
CC       {ECO:0000269|PubMed:10347026}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
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DR   EMBL; Y18586; CAB46229.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Y865; -.
DR   SMR; Q9Y865; -.
DR   STRING; 5061.CADANGAP00002564; -.
DR   ChEMBL; CHEMBL5085; -.
DR   CAZy; GH27; Glycoside Hydrolase Family 27.
DR   CLAE; MEL27B_ASPNG; -.
DR   VEuPathDB; FungiDB:An02g11150; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1145000; -.
DR   VEuPathDB; FungiDB:ATCC64974_53780; -.
DR   VEuPathDB; FungiDB:M747DRAFT_293587; -.
DR   eggNOG; KOG2366; Eukaryota.
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..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..443
FT                   /note="Probable alpha-galactosidase B"
FT                   /id="PRO_0000393218"
FT   ACT_SITE        149
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        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        156
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        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        212
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        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        39..71
FT                   /evidence="ECO:0000250"
FT   DISULFID        121..151
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   443 AA;  48784 MW;  187B7401084D4D99 CRC64;
     MRWLLTSSAL LVPAAALVRP DGVGLTPALG WNSWNAYSCD IDADKIVTAA NEVVNLGLKD
     LGYEYINIDD CWSVKSGRNT TTKRIIPDPD KFPNGISGVA DQVHALGLKL GIYSSAGLTT
     CAGYPASLGY EEIDAQSFAE WGIDYLKYDN CGVPTNLTDQ YTYCVPDSTD GSNYPNGTCV
     NLTDAAPQGY DWATSTTAKR YQRMRDALLS VNRTILYSLC DWGQADVNAW GNATGNSWRM
     SGDITATWSR IAEIANENSF LMNYANFWGY PDPDMLEVGN GNLTLPENRA HFALWAMMKA
     PLIIGTPLDS IDTSHLTILS NKPLLTFHQD AVIGRPAYPY KWGYNPDWTF DPEHPAEYWS
     GPTSSGEVFV LMLNSEGEVK TRSAVWEEVP ELKDRGTKKN SKEKKGFKVT DAWTGKDLGC
     VKDKYEVKLQ AHDVAVLVVG GQC