ID   MEL_SACMI               Reviewed;         471 AA.
AC   Q11129;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Alpha-galactosidase;
DE            EC=3.2.1.22;
DE   AltName: Full=Alpha-D-galactoside galactohydrolase;
DE   AltName: Full=MELj;
DE   AltName: Full=Melibiase;
DE   Flags: Precursor;
GN   Name=MEL;
OS   Saccharomyces mikatae (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=114525;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NBRC 1816;
RX   PubMed=9003294; DOI=10.1007/s004380050303;
RA   Naumova E.S., Turakainen H., Naumov G.I., Korhola M.;
RT   "Superfamily of alpha-galactosidase MEL genes of the Saccharomyces sensu
RT   stricto species complex.";
RL   Mol. Gen. Genet. 253:111-117(1996).
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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
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DR   EMBL; X95506; CAA64760.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q11129; -.
DR   SMR; Q11129; -.
DR   CAZy; GH27; Glycoside Hydrolase Family 27.
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; IPR006215; Glyco_hydro_melibiase.
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   PRINTS; PR00740; GLHYDRLASE27.
DR   PRINTS; PR00748; MELIBIASE.
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..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..471
FT                   /note="Alpha-galactosidase"
FT                   /id="PRO_0000001007"
FT   ACT_SITE        149
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        209
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        270
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        361
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        370
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        417
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        422
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        435
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        454
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        42..74
FT                   /evidence="ECO:0000250"
FT   DISULFID        121..151
FT                   /evidence="ECO:0000250"
FT   DISULFID        221..237
FT                   /evidence="ECO:0000250"
FT   DISULFID        223..230
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   471 AA;  52378 MW;  9FFF2FA03C03872A CRC64;
     MSYIYLFITA AAVTGALGSS PSYNGLGLTP QMGWDNWNTF ACDVSEQLLL NTADRISEIG
     LKDLGYKYVI LDDCWSSGRN SNGTLVADKN KFPNGMDHVA RHLHNNNFLF GMYSSAGEYT
     CAGYPGSLGH EQEDAEFFAR NGVDYLKYDN CYNKGKFGTP ETSYKRYKAM SDALNKTGRP
     IFYSLCNWGQ DLTFYWGSDI ANSWRMSGDI YPEFDRPDSR CPCDGDQYDC SYAGFHCSIM
     NILNKAAPMG QNAGIGGWND LDNLEVGVGN LTDDEEKAHF SMWAMVKSPL IIGADVNHLK
     ESSYSIYSQA SVIAINQDPK GVPATRVWRH YVSQTDKYGK GEIQLWSCPL DNGDQVIALL
     NGSNKKRPMN ASLEDIFFDS YLGSEELSSS WDIYDLWANR IDNTIASNIL KNNKVTNSSL
     YNATELSYKE GLSKNDTRLF GVQIGTVSPG GLLNTTVPAH GVALYRLRRS R