ID   MEL_ZYGMR               Reviewed;         470 AA.
AC   Q9P4V4;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Alpha-galactosidase;
DE            EC=3.2.1.22;
DE   AltName: Full=Alpha-D-galactoside galactohydrolase;
DE   AltName: Full=MELr;
DE   AltName: Full=Melibiase;
DE   Flags: Precursor;
GN   Name=MEL;
OS   Zygotorulaspora mrakii (Zygosaccharomyces mrakii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygotorulaspora.
OX   NCBI_TaxID=42260;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 36242 / CBS 4218 / JCM 1800 / NBRC 1835 / NRRL Y-12654 / VTT
RC   C-94202;
RX   PubMed=10915212; DOI=10.1007/s002840010123;
RA   Oda Y., Fujisawa T.;
RT   "Nucleotide sequence of alpha-galactosidase MEL gene from Zygosaccharomyces
RT   mrakii.";
RL   Curr. Microbiol. 41:220-222(2000).
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; AB030209; BAA99555.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9P4V4; -.
DR   SMR; Q9P4V4; -.
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:0000255"
FT   CHAIN           19..470
FT                   /note="Alpha-galactosidase"
FT                   /id="PRO_0000001012"
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        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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        388
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   470 AA;  51912 MW;  232ACAE756DF432E CRC64;
     MFSLLLLTST ALVETALGVS PSYNGLGLTP QMGWNNWNTF ACNVTEQLLL GTADRISELG
     LKDVGYNYVI LDDCWSGGRS SNGSLVPDLN KFPHGMKYVA DHLHDQDLLF GMYSSAGEYT
     CAGYPGSLGH EEKDAQFFAR NEVDYLKYDN CYNKGQFGTP QASYERYKAM SDALNNTGRP
     IFYSLCNWGQ DLTFYWGSAI ANSWRMSGDI TADFDRPDSR CPCGDDEYDC KYAGYHCSIM
     NILNKAAPMG QNANPGGWND LDMLEVGVGN LTDDEEKAHF SMWAMVRSPL IIGADVNHLK
     PSSFSIYAQS PVIAINQDPR GVPATRVWRR QVSDTDAYGR GEVQFWSGPL ENGDQVIAFL
     NGGNRMRPMN AGLDDIFFDS HPGAPELNST WAVYDLWANR MEDSVASDIL NGNRSSNGLL
     YNSTQQSYSQ GLARNDSRLF GSQIGTIQAG GRLNVTVPAH GVGLYRLRLQ