ID   MEL_TORDE               Reviewed;         474 AA.
AC   Q9UVD6;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Alpha-galactosidase;
DE            EC=3.2.1.22;
DE   AltName: Full=Alpha-D-galactoside galactohydrolase;
DE   AltName: Full=MELt;
DE   AltName: Full=Melibiase;
DE   Flags: Precursor;
GN   Name=MEL;
OS   Torulaspora delbrueckii (Yeast) (Candida colliculosa).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Torulaspora.
OX   NCBI_TaxID=4950;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NBRC 1255 / IAM 4952;
RX   PubMed=10590467;
RX   DOI=10.1002/(sici)1097-0061(199912)15:16<1797::aid-yea498>3.0.co;2-g;
RA   Oda Y., Fukunaga M.;
RT   "Isolation and characterization of MELt gene from Torulaspora delbrueckii
RT   IFO 1255.";
RL   Yeast 15:1797-1801(1999).
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; AB027130; BAA86883.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9UVD6; -.
DR   SMR; Q9UVD6; -.
DR   CAZy; GH27; Glycoside Hydrolase Family 27.
DR   CLAE; MEL27A_TORDE; -.
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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..474
FT                   /note="Alpha-galactosidase"
FT                   /id="PRO_0000001010"
FT   ACT_SITE        150
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        210
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        414
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        436
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        455
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        43..75
FT                   /evidence="ECO:0000250"
FT   DISULFID        122..152
FT                   /evidence="ECO:0000250"
FT   DISULFID        222..238
FT                   /evidence="ECO:0000250"
FT   DISULFID        224..231
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   474 AA;  52364 MW;  6F058455B3A3D7B1 CRC64;
     MINFSLLTSI VLLASKVVGV SPSYNGLGLT PQMGWNNWNT FACNVSEDLL LSTVDRIAAL
     GLRDIGYHYV ILDDCWSDGR DSDGMLVPDS TKFPNGMKHV ADYLHGKDFL FGMYSSAGEY
     TCAGYAGSLD HEEDDAAFFA KNEVDYLKYD NCYNRGQFGT PETSFNRYRA MSEALNKTER
     PIFYSLCNWG QDLTFYWGSG IANSWRISGD ITAEFDRPDS RCPCDGDEYD CPYAGFHCSI
     MNILNKAAPM GQNAGVGGWN DLDCLEVGVG NLTDDEEKAH FSMWAIVKSA MVIGADVRNL
     KPSSFSIYSQ ASVLAINQDP AGAPAIRVWR RYVPETDQHG QGEVQLWSGP LDNGDRVVAL
     LNGGAKERPM VAYLEDIFID SFVGSEELSS TWNVYDLWAN RIDDSTASQI LVGNRTANGL
     LYNATQLSYA DGLKANDTRL FGEKVGTIEP YGLLNVTVPA HGVGLFRLRR ESRK