ID   MEL_SACCA               Reviewed;         471 AA.
AC   Q03647;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Alpha-galactosidase;
DE            EC=3.2.1.22;
DE   AltName: Full=Alpha-D-galactoside galactohydrolase;
DE   AltName: Full=MELx;
DE   AltName: Full=Melibiase;
DE   Flags: Precursor;
GN   Name=MEL;
OS   Saccharomyces pastorianus (strain ATCC 76529 / Carlsberg bottom yeast no.1
OS   / CBS 1513 / CLIB 176 / NBRC 1167 / NCYC 396 / NRRL Y-12693) (Saaz-type
OS   lager yeast) (Saccharomyces carlsbergensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=1073566;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 76529 / Carlsberg bottom yeast no.1 / CBS 1513 / CLIB 176 /
RC   NBRC 1167 / NCYC 396 / NRRL Y-12693;
RX   PubMed=1711992; DOI=10.1016/0378-1119(91)90229-5;
RA   Turakainen H., Korhola M., Aho S.;
RT   "Cloning sequence and chromosomal location of a MEL gene from Saccharomyces
RT   carlsbergenesis NCYC396.";
RL   Gene 101:97-104(1991).
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; M58484; AAA34769.1; -; Genomic_DNA.
DR   PIR; JQ1021; JQ1021.
DR   AlphaFoldDB; Q03647; -.
DR   SMR; Q03647; -.
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; 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.
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_0000001009"
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        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        412
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;  52000 MW;  E49E27EC278C4A23 CRC64;
     MFLLYLFTSF AAVSGVLGSS PSYNGLGLTP QMGWDNWNTF ACDVSEQLLL DTADRISEIG
     LKDLGYTYVI LDDCWSSGRT ANGTLVADKE KFPNGMSHVA DHLHNNNFLF GMYSSAGEYT
     CAGYPGSLGH EEEDAEFFAS NGVDYLKYDN CYNKGQFGAP ETSYKRYKAM SDALNKTGRP
     IFYSLCNWGQ DLTHYWGSDI ANSWRMSGDI YPQFTRPDSR CPCDGDQFDC AYAGFHCSIM
     NILNKAAPMG QNAGIGGWND LDNLEVGVGN LTDDEEKAHF SMWAMVKSPL VIGADVNHLK
     ASSYSIYSQA SVIAINQDPK GVPATRVWRH QVPQTDKYGQ GEIQFWSGPL DNGDQVIALL
     NGGIKPRPMN TNLEEIFFDS YLGFEQLSSN WDIYDLWANR VDNATSANIL NNNSVGNATI
     YNATALSYKD GMAKNDTRLF GTKIGSISPD GLLNTTVPAH GIAFYRLRRS T