ID   AGAL_CYATE              Reviewed;         411 AA.
AC   P14749;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 97.
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   Cyamopsis tetragonoloba (Guar) (Cluster bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Indigofereae; Cyamopsis.
OX   NCBI_TaxID=3832;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Aleurone;
RX   PubMed=2577496; DOI=10.1007/bf00027314;
RA   Overbeeke N., Fellinger A.J., Toonen M.Y., van Wassenaar D., Verrips C.T.;
RT   "Cloning and nucleotide sequence of the alpha-galactosidase cDNA from
RT   Cyamopsis tetragonoloba (guar).";
RL   Plant Mol. Biol. 13:541-550(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 48-57 AND 172-178.
RC   TISSUE=Seed;
RX   AGRICOLA=IND91035194; DOI=10.1007/BF00019518;
RA   Hughes S.G., Overbeeke N., Robinson S., Pollock K., Smeets F.L.M.;
RT   "Messenger RNA from isolated aleurone cells directs the synthesis of an
RT   alpha-galactosidase found in the endosperm during germination of guar
RT   (Cyamopsis tetragonaloba) seed.";
RL   Plant Mol. Biol. 11:783-789(1988).
CC   -!- FUNCTION: 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.
CC       Preferentially cleaves alpha-1,6 glycoside linkages.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
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DR   EMBL; X14619; CAA32772.1; -; mRNA.
DR   PIR; S07472; S07472.
DR   AlphaFoldDB; P14749; -.
DR   SMR; P14749; -.
DR   CAZy; GH27; Glycoside Hydrolase Family 27.
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; Glycoprotein; Glycosidase;
KW   Hydrolase; Signal.
FT   SIGNAL          1..24
FT   PROPEP          25..47
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="PRO_0000001002"
FT   CHAIN           48..411
FT                   /note="Alpha-galactosidase"
FT                   /id="PRO_0000001003"
FT   ACT_SITE        177
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        232
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         210..214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        32
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        68..100
FT                   /evidence="ECO:0000250"
FT   DISULFID        148..179
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   411 AA;  45136 MW;  5B1715858D1AB11E CRC64;
     MATHYSIIGG MIIVVLLMII GSEGGRLLEK KNRTSAEAEH YNVRRYLAEN GLGQTPPMGW
     NSWNHFGCDI NENVVRETAD AMVSTGLAAL GYQYINLDDC WAELNRDSEG NMVPNAAAFP
     SGIKALADYV HSKGLKLGVY SDAGNQTCSK RMPGSLGHEE QDAKTFASWG VDYLKYDNCE
     NLGISVKERY PPMGKALLSS GRPIFFSMCE WGWEDPQIWA KSIGNSWRTT GDIEDNWNSM
     TSIADSNDKW ASYAGPGGWN DPDMLEVGNG GMTTEEYRSH FSIWALAKAP LLVGCDIRAM
     DDTTHELISN AEVIAVNQDK LGVQGKKVKS TNDLEVWAGP LSDNKVAVIL WNRSSSRATV
     TASWSDIGLQ QGTTVDARDL WEHSTQSLVS GEISAEIDSH ACKMYVLTPR S