ID   MEL2_YEASX              Reviewed;         471 AA.
AC   P41945;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 95.
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=MEL2;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7725791; DOI=10.1002/yea.320101205;
RA   Turakainen H., Kristo P., Korhola M.;
RT   "Consideration of the evolution of the Saccharomyces cerevisiae MEL gene
RT   family on the basis of the nucleotide sequences of the genes and their
RT   flanking regions.";
RL   Yeast 10:1559-1568(1994).
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; Z37508; CAA85737.1; -; Genomic_DNA.
DR   PIR; S50310; S50310.
DR   AlphaFoldDB; P41945; -.
DR   SMR; P41945; -.
DR   GlyCosmos; P41945; 9 sites, No reported glycans.
DR   SGD; S000029663; MEL2.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProtKB-ARBA.
DR   CDD; cd14792; GH27; 1.
DR   FunFam; 3.20.20.70:FF:000202; Alpha-galactosidase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR017853; GH_hydrolase_sf.
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; IPR041233; Melibiase_C.
DR   PANTHER; PTHR11452:SF75; ALPHA-GALACTOSIDASE MEL1; 1.
DR   PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1.
DR   Pfam; PF16499; Melibiase_2; 1.
DR   Pfam; PF17801; Melibiase_C; 1.
DR   PRINTS; PR00740; GLHYDRLASE27.
DR   PRINTS; PR00748; MELIBIASE.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 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 2"
FT                   /id="PRO_0000001014"
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        105
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        370
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        413
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;  52230 MW;  7FA36066BE01F33B CRC64;
     MFAFYFLTAC ISLKGVFGVS PSYNGLGLTP QMGWDNWNTF ACDVSEQLLL DTADRISDLG
     LKDMGYKYII LDDCWSSGRD SDGFLVADEQ KFPNGMGHVA DHLHNNSFLF GMYSSAGEYT
     CAGYPGSLGR EEEDAQFFAN NRVDYLKYDN CYNKGQFGTP EISYHRYKAM SDALNKTGRP
     IFYSLCNWGQ DLTFYWGSGI ANSWRMSGDI TAEFTRPDSR CPCDGDEYDC KYAGFHCSIM
     NILNKAAPMG QNAGVGGWND LDNLEVRVGN LTDDEEKAHF PMWAMVKSPL IIGADVNTLK
     PSSYSIYSQA SVIAINQDPK GIPATRVWRY YVSDTDEYGQ GEIQMWSGPL DNGDQVVALL
     NGGSVPRPMN TTLEEIFFDS NLGSKELTST WDIYDLWANR VDNSTASAIL GQNKTATGIL
     YNATEQSYKD GLSKNDTRLF GQKIGSLSPN AILNTTVPAH GIAFYRLRPS A
//