ID   AGAL3_HYPJE             Reviewed;         624 AA.
AC   Q92451;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Alpha-galactosidase 3;
DE            EC=3.2.1.22;
DE   AltName: Full=Alpha-D-galactoside galactohydrolase 3;
DE   AltName: Full=Melibiase 3;
DE   Flags: Precursor;
GN   Name=agl3;
OS   Hypocrea jecorina (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=51453;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 56765 / Rut C-30;
RX   PubMed=8797842; DOI=10.1111/j.1432-1033.1996.0104h.x;
RA   Margolles-Clark E., Tenkanen M., Luonteri E., Penttila M.;
RT   "Three alpha-galactosidase genes of Trichoderma reesei cloned by expression
RT   in yeast.";
RL   Eur. J. Biochem. 240:104-111(1996).
CC   -!- FUNCTION: Alpha-galactosidase involved in the degradation of simple
CC       oligosaccharides like melibiose, raffinose and stachyose, and of
CC       polymeric galacto(gluco)mannans. {ECO:0000269|PubMed:8797842}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 3.5-4.5. {ECO:0000269|PubMed:8797842};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z69255; CAA93246.1; -; mRNA.
DR   PIR; S74222; S74222.
DR   AlphaFoldDB; Q92451; -.
DR   SMR; Q92451; -.
DR   CAZy; GH27; Glycoside Hydrolase Family 27.
DR   CLAE; MEL27C_TRIRE; -.
DR   VEuPathDB; FungiDB:TrQ_006770; -.
DR   OMA; QWASWGV; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IDA:UniProtKB.
DR   GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 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; 1.
DR   Pfam; PF17801; Melibiase_C; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..624
FT                   /note="Alpha-galactosidase 3"
FT                   /id="PRO_5000147669"
FT   ACT_SITE        347
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        412
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        393
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        469
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   624 AA;  68455 MW;  9454A5C932040D73 CRC64;
     MSPSAAVLIP LAAAVLLRPV VGQTQCGGNL YTPGTLNFTL ECYNAFQDCV AQFEANASQV
     DCNDGKGNLF MQQQANLGAS PGSQNNDAII AFQDIRDLCL LSGSTTATWG YSDNQWYWAA
     AEDACYTNDP TRTDVVKTHP APFCIQNRDS SLPECYPQPD ATPPGGPLKV IKTAKTRNGF
     KSSARGWNTY GVQALVNGSQ VVPSFAGQSG LFYTQKFVET QCGVLARPEF KKAGYDLCSL
     DSGWQATTAV DQHGRIIYNT TRFNLPELAS WLHKRDLKLG VYITPGVPCL AHNQTILGTN
     IKIKDVLNGN NDQINCDFDF RKDGVQQWHD SVVAQWASWG VDMLKLDFLT PGSPSNGANL
     ACDSSDAVRA YQKAIKKSGR KIRLDISWKL CRNETWLPIW SDLAESMRTD QDLDNYGTNT
     LMAWQVGQRA IENYRQYIGL QAQRNVPLTI YPDMDALFTV NPEHLAGVND TIRYTVQNHW
     LGAGANLIIG GDMEQVDALG LKLTTSKQSI DAADFFAKYP MQPRNPGTGS NAAKQLQAWI
     GGPSDDHEAY VLIVNYGPDL GNGGFSTKLY GKQKVTVSLK DLGISGSAWT FTDIWSGKSS
     RVTGSYSAWL TEGESQLLRL KRTH