ID   MEL_LACCI               Reviewed;         469 AA.
AC   Q99172;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Alpha-galactosidase;
DE            EC=3.2.1.22;
DE   AltName: Full=Alpha-D-galactoside galactohydrolase;
DE   AltName: Full=Melibiase;
DE   Flags: Precursor;
GN   Name=MEL;
OS   Lachancea cidri (Yeast) (Zygosaccharomyces cidri).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=29831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7975892; DOI=10.1002/yea.320100605;
RA   Turakainen H., Hankaanpaa M., Korhola M., Aho S.;
RT   "Characterization of MEL genes in the genus Zygosaccharomyces.";
RL   Yeast 10:733-745(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; L24957; AAA35280.1; -; Genomic_DNA.
DR   PIR; S45453; S45453.
DR   AlphaFoldDB; Q99172; -.
DR   SMR; Q99172; -.
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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..469
FT                   /note="Alpha-galactosidase"
FT                   /id="PRO_0000001011"
FT   ACT_SITE        148
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        208
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        369
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        402
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        421
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        426
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        434
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        41..73
FT                   /evidence="ECO:0000250"
FT   DISULFID        120..150
FT                   /evidence="ECO:0000250"
FT   DISULFID        220..236
FT                   /evidence="ECO:0000250"
FT   DISULFID        222..229
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   469 AA;  51737 MW;  1720331848F46594 CRC64;
     MFPFFFALFF SSTDVLAASP SYNGLGLTPQ MGWDNWNSFG CSVKEELLLG TAEKIVKLGL
     KDLGYNYIIL DDCWSSGRSS NGSLLADDSK FPHGMKYVAE QLHNSQLKFG MYSSAGEYTC
     AGYAGSLGYE DMDAATFASW DVDYLKYDNC YNKGEFGTPE ISYKRYKAMS DALNKTGRPI
     FYSLCNWGQD LTFYWGSAIS NSWRMSGDVY PQFDRPDSRC PCSGDEYDCS YPGFHCSIMN
     ILNKAAPMGQ NAAPGGWNDL DMLEVGVGNM SDSEEVAHFS MWAIVKSPLI IGADIDDLKD
     SSLSVYSNPA VIAINQDVLG TPATRIWKYH VSDKDQYGEG EIQLWSGPLD NGDHVVALLN
     GGNNERSMNA SWNDIFIDYL ADSDELSNTW GLYDLWARRM SNATAASILS GNMTSAGLNY
     NVTQLNYTAG IARNDSRLFG DRVVELSKGE SLTATVPGHG VALFRLRPE