ID   AGAL_COFAR              Reviewed;         378 AA.
AC   Q42656;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 91.
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;
OS   Coffea arabica (Arabian coffee).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Gardenieae complex;
OC   Bertiereae - Coffeeae clade; Coffeeae; Coffea.
OX   NCBI_TaxID=13443;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 16-34; 215-231 AND
RP   373-378.
RC   TISSUE=Seed;
RX   PubMed=8144030; DOI=10.1016/0378-1119(94)90548-7;
RA   Zhu A., Goldstein J.;
RT   "Cloning and functional expression of a cDNA encoding coffee bean alpha-
RT   galactosidase.";
RL   Gene 140:227-231(1994).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=8619622; DOI=10.1006/abbi.1996.0129;
RA   Zhu A., Leng L., Monahan C., Zhang Z., Hurst R., Lenny L., Goldstein J.;
RT   "Characterization of recombinant alpha-galactosidase for use in
RT   seroconversion from blood group B to O of human erythrocytes.";
RL   Arch. Biochem. Biophys. 327:324-329(1996).
RN   [3]
RP   BIOTECHNOLOGY.
RX   PubMed=11099655; DOI=10.1046/j.1537-2995.2000.40111290.x;
RA   Kruskall M.S., AuBuchon J.P., Anthony K.Y., Herschel L., Pickard C.,
RA   Biehl R., Horowitz M., Brambilla D.J., Popovsky M.A.;
RT   "Transfusion to blood group A and O patients of group B RBCs that have been
RT   enzymatically converted to group O.";
RL   Transfusion 40:1290-1298(2000).
RN   [4]
RP   BIOTECHNOLOGY.
RX   PubMed=17637242;
RA   Zhang Y.P., Gong F., Bao G.Q., Gao H.W., Ji S.P., Tan Y.X., Li S.B.,
RA   Li L.L., Wang Y.L., Xu H., Xu L.J., Tian S.G., Zhang Z.X., Lu Q.S., Qiu Y.,
RA   Bai J.S., Chen J.T.;
RT   "B to O erythrocyte conversion by the recombinant alpha-galactosidase.";
RL   Chin. Med. J. 120:1145-1150(2007).
CC   -!- FUNCTION: Preferentially cleaves alpha-1,3 and alpha-1,4 glycoside
CC       linkages. Involved in the hydrolysis of the galactomannan, it splits
CC       alpha-linked galactose moieties. It is particularly suitable for the
CC       hydrolysis of guar gum to a gum with improved gelling properties. Can
CC       cleave terminal alpha-1,3-linked galactose residues responsible for
CC       blood group B specificity from the surface of erythrocytes thereby
CC       converting these cells serologically to group O.
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   -!- BIOTECHNOLOGY: Used to convert human blood group antigens of type B
CC       into type O, the universal donor type. {ECO:0000269|PubMed:11099655,
CC       ECO:0000269|PubMed:17637242, ECO:0000269|PubMed:8619622}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
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DR   EMBL; L27992; AAA33022.1; -; mRNA.
DR   PIR; T50781; T50781.
DR   AlphaFoldDB; Q42656; -.
DR   SMR; Q42656; -.
DR   BindingDB; Q42656; -.
DR   ChEMBL; CHEMBL5217; -.
DR   DrugCentral; Q42656; -.
DR   CAZy; GH27; Glycoside Hydrolase Family 27.
DR   Proteomes; UP000515148; Genome assembly.
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; 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   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Reference proteome; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000269|PubMed:8144030"
FT   CHAIN           16..378
FT                   /note="Alpha-galactosidase"
FT                   /id="PRO_0000001001"
FT   ACT_SITE        145
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        200
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         178..182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        36..68
FT                   /evidence="ECO:0000250"
FT   DISULFID        116..147
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   378 AA;  41310 MW;  9FC7610BFD760AE3 CRC64;
     MVKSPGTEDY TRRSLLANGL GLTPPMGWNS WNHFRCNLDE KLIRETADAM VSKGLAALGY
     KYINLDDCWA ELNRDSQGNL VPKGSTFPSG IKALADYVHS KGLKLGIYSD AGTQTCSKTM
     PGSLGHEEQD AKTFASWGVD YLKYDNCNNN NISPKERYPI MSKALLNSGR SIFFSLCEWG
     EEDPATWAKE VGNSWRTTGD IDDSWSSMTS RADMNDKWAS YAGPGGWNDP DMLEVGNGGM
     TTTEYRSHFS IWALAKAPLL IGCDIRSMDG ATFQLLSNAE VIAVNQDKLG VQGNKVKTYG
     DLEVWAGPLS GKRVAVALWN RGSSTATITA YWSDVGLPST AVVNARDLWA HSTEKSVKGQ
     ISAAVDAHDS KMYVLTPQ