ID   AGALC_ASPOR             Reviewed;         751 AA.
AC   Q2TW69;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Probable alpha-galactosidase C;
DE            EC=3.2.1.22;
DE   AltName: Full=Melibiase C;
DE   Flags: Precursor;
GN   Name=aglC; ORFNames=AO090010000684;
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 36 family. {ECO:0000305}.
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DR   EMBL; AP007175; BAE66504.1; -; Genomic_DNA.
DR   RefSeq; XP_001827637.2; XM_001827585.2.
DR   AlphaFoldDB; Q2TW69; -.
DR   SMR; Q2TW69; -.
DR   STRING; 510516.Q2TW69; -.
DR   CAZy; GH36; Glycoside Hydrolase Family 36.
DR   EnsemblFungi; BAE66504; BAE66504; AO090010000684.
DR   GeneID; 5999771; -.
DR   KEGG; aor:AO090010000684; -.
DR   VEuPathDB; FungiDB:AO090010000684; -.
DR   HOGENOM; CLU_009640_2_1_1; -.
DR   OMA; WEGIYFD; -.
DR   Proteomes; UP000006564; Chromosome 8.
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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd14791; GH36; 1.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 2.70.98.60; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR038417; Alpga-gal_N_sf.
DR   InterPro; IPR000111; Glyco_hydro_27/36_CS.
DR   InterPro; IPR002252; Glyco_hydro_36.
DR   InterPro; IPR031705; Glyco_hydro_36_C.
DR   InterPro; IPR031704; Glyco_hydro_36_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF16874; Glyco_hydro_36C; 1.
DR   Pfam; PF16875; Glyco_hydro_36N; 1.
DR   PIRSF; PIRSF005536; Agal; 1.
DR   PRINTS; PR00743; GLHYDRLASE36.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase; Magnesium;
KW   NAD; Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..751
FT                   /note="Probable alpha-galactosidase C"
FT                   /id="PRO_0000395065"
FT   ACT_SITE        510
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ALJ4"
FT   ACT_SITE        572
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ALJ4"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        433
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        452
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        500
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        720
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   751 AA;  82879 MW;  9991719A9ED0A506 CRC64;
     MFGSPKRAAL AAASLLAVFG NGPSVMAQET SSNNAVVADG KTFALNGENV SYRFRVNETT
     GDLVSDHFGG SITGNLFPGF GAEALGGWVG LAGRFRREFP DHGRGDFRIP AVRIRQEAGY
     TVTDLQYQSY SVIPGKPALP GLPSTFGSEE DVTTLVVHLY DNYSSIAVDL SYSIFPKYDA
     IVRSANVTNK GTQNITVEAL SSFSFDFPYE DLEMISLRGD WAREAHRQRR KVEYGLQGFG
     SSTGFSSHLH NPFLAIVHPS TTESQGEAWG FNLVYTGSFS VDVEKGSQGL TRALLGFNPS
     QLSWQLGAGE TLTSPECVSV YSSDGIGGMS RSFHRLYRNH LIKSKFATSD RPPLLNSWEG
     LYFDYNESTI YRLAEESAAL GVKLFVMDDG WFGDKYPRVS DNAGLGDWVP NPDRFPDGLT
     PLVEDVTKLK AGNSSTDLRF GLWVEPEMAN PNSTLYHEHP DWVLHAGQYP RTLQRNQLVL
     NLALPEVQDY IIDEITNILN SSAISYVKWD FNRAMHETPS PSNDHEYILG MYRVFDTLTT
     RFPDVLWEGC ASGGGRFDPG VLEYFPQIWT SDNTDALMRI TIQLGTSLAY PPSAMGAHLS
     AVPNAQTGRT IPVKFRGHVA MMGGSFGLEL DPAELQEDEK AEVPGLIALA EKVNPIILTG
     DMWRLRLPEE SNWPAVLFIS EDGNQAVLFY FQLGPNVNHA TPWLRLQGLD PKATYSVDGN
     GSYSGATLMN MGLQYKFESD YDSKVVFLQK Q