ID   AGALB_ASPFC             Reviewed;         426 AA.
AC   B0Y224;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Probable alpha-galactosidase B;
DE            EC=3.2.1.22;
DE   AltName: Full=Melibiase B;
DE   Flags: Precursor;
GN   Name=aglB; ORFNames=AFUB_050660;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499597; EDP51064.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y224; -.
DR   SMR; B0Y224; -.
DR   EnsemblFungi; EDP51064; EDP51064; AFUB_050660.
DR   HOGENOM; CLU_013093_2_2_1; -.
DR   PhylomeDB; B0Y224; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
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..13
FT                   /evidence="ECO:0000255"
FT   CHAIN           14..426
FT                   /note="Probable alpha-galactosidase B"
FT                   /id="PRO_0000393215"
FT   ACT_SITE        134
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        226
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         204..208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        215
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        24..56
FT                   /evidence="ECO:0000250"
FT   DISULFID        106..136
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   426 AA;  47215 MW;  5CB8CBBEADB62F63 CRC64;
     MSRSKTRQGK LPALGWNTWN AFGCDIDATK IMTAANEVVN LGLKDLGYEY INIDDCWSVK
     SGRDASTQRI IPDPDKFPDG ISGVADQIHD LGLKIGIYSS AGLTTCAGYP ASLGYEDIDA
     QTFAEWGIDY LKYDNCGVPS NWTDTYTYCV PDPGSKATNG TCPDNKNPAP AGYDWRTSLT
     AERYRRMRDA LVSVDRTILY SLCEWGQANV NDWGNETGNS WRTTGDITPS WPRIAAIANE
     NSFLMNHVDF WGYPDPDMLE VGNGNLTLAE NRAHFALWAA MKSPLIIGTA LDSISQDHLA
     ILSNKILLKF HQDPVIGRPA QPYKWGYNPD WTFDPAHPAE YWSGASSVLG GTLVLMLNSE
     DTTQRRTAVW KEVPELKDVL GRQGKRRIGF RVTDVWTGKD LGCVRDHYSV ELESHDVAAL
     VVGRAC