ID   AGALB_ASPOR             Reviewed;         442 AA.
AC   Q2UJ97;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=AO090003001305;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007155; BAE58368.1; -; Genomic_DNA.
DR   RefSeq; XP_001820370.1; XM_001820318.2.
DR   AlphaFoldDB; Q2UJ97; -.
DR   SMR; Q2UJ97; -.
DR   STRING; 510516.Q2UJ97; -.
DR   CAZy; GH27; Glycoside Hydrolase Family 27.
DR   EnsemblFungi; BAE58368; BAE58368; AO090003001305.
DR   GeneID; 5992593; -.
DR   KEGG; aor:AO090003001305; -.
DR   VEuPathDB; FungiDB:AO090003001305; -.
DR   HOGENOM; CLU_013093_2_2_1; -.
DR   OMA; NAFGCDI; -.
DR   Proteomes; UP000006564; Chromosome 2.
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; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..442
FT                   /note="Probable alpha-galactosidase B"
FT                   /id="PRO_0000393219"
FT   ACT_SITE        152
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        246
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         224..228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        179
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        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        42..74
FT                   /evidence="ECO:0000250"
FT   DISULFID        124..154
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   442 AA;  48507 MW;  8E830340213C3A65 CRC64;
     MQRYISLSVS LSLLSGANAL VRPDGVGRLP ALGWNTWNAF GCDIDASKVL TAAEETINLG
     LKDAGYEYIN IDDCWSVKSG RDPNTKRIIP DSAKFPDGIS GVASKIHDLG LKVGIYSSAG
     TETCAGYPAS LGYEKIDAES FAEWGIDYLK YDNCGVPTNW TDTYTHCVPD NSNGSKFPNG
     TCPDISNPAP TAYDWSSSNT AQRYNAMRDA LLGVNRTILY SLCEWGQADV NTWGNGTGNS
     WRTTGDITPD WSRIVEIANE NSFLMNYADF WGYPDPDMLE VGNGNLTLEE NRAHFALWAA
     MKSPLIIGTA LDSINEEHLA ILKNKPLLSF HQDPVIGRPA YPYKWGYNPD WTFDPAHPAE
     YWSGPSSTLG GTLVLMFNSE DSAKHRTAVW SEIPELKDSA EKGSGYRVTE IWTGEDLGCV
     KDQYDVELQS HDIAALVVGE SC