ID   AGAL2_HYPJE             Reviewed;         746 AA.
AC   Q92457;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Alpha-galactosidase 2;
DE            EC=3.2.1.22;
DE   AltName: Full=Alpha-D-galactoside galactohydrolase 2;
DE   AltName: Full=Melibiase 2;
DE   Flags: Precursor;
GN   Name=agl2;
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}.
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DR   EMBL; Z69254; CAA93245.1; -; mRNA.
DR   PIR; S74219; S74219.
DR   AlphaFoldDB; Q92457; -.
DR   SMR; Q92457; -.
DR   CAZy; GH36; Glycoside Hydrolase Family 36.
DR   CLAE; MEL36B_TRIRE; -.
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:0016052; P:carbohydrate catabolic process; IEA:InterPro.
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   1: Evidence at protein level;
KW   Glycoprotein; Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..746
FT                   /note="Alpha-galactosidase 2"
FT                   /id="PRO_5000147668"
FT   ACT_SITE        504
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ALJ4"
FT   ACT_SITE        566
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ALJ4"
FT   CARBOHYD        43
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        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        360
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        427
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        446
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        495
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        714
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   746 AA;  82079 MW;  7735B56D7AD3B838 CRC64;
     MLGAPSPRRL ADVLAVTAGL VASVRAASPI SVSGKSFALN GDNVSYRFHV DDDSKDLIGD
     HFGGPATEDG VFPPIIGPIQ GWVDLIGRQR REFPDLGRGD FRTPAVHIRQ AAGYTVSDFQ
     YKSHRVVEGK PALRGLPSTF GDAGDVSTLV VHMYDNYSSV AADLTYSIFP KYDAIVRSVN
     ITNMGKGNIT IEKLASLSVD LPYEDFDMLE LKGDWAREGK RLRRKVDYGS QGFGSTTGYS
     SHLHNPFFSL ITPTTTESQG EAWGFSLVYT GSFSVEVEKG SQGLTRAAIG VNPYQLSWPL
     GPGETFSSPE AVAVFSTTGV GGMSRKFHNL YRKHLIKSKF ATQMHPVLLN SWEGLGFDYN
     DTTILHLAQE SADLGIKLFV LDDGWFGVKH PRVSDNAGLG DWEANPKRFP QGLPDFISDV
     TKLKVANSSD HLQFGLWFEP EMVNPNSTLY MEHPDWAIHA GSYPRTLTRN QLVLNVALPE
     VQDFIIESLS NILSNASISY VKWDNNRGIH EAPYPGLDYA YMLGLYRVFD TLSSKFPNVR
     WEGCASGGGR FDPGVLQYFP HIWTSDDTDA VERIAIQFGT SLVYPPSAMG AHVSAVPNGQ
     TQRTTSIAFR AHVAMMGGSF GFELTPAEMP EDDKAQIPGI IALAEKVNPI VVKGDMWRLS
     LPEESNWPAA LFISQDGSQA VLFYFQIRAN INNAWPVLRL QGLDASAKYK IDGNQTFSGA
     TLMNIGLQYQ FNGDYDSKVV FLEKQT