ID   AGAL_ORYSJ              Reviewed;         417 AA.
AC   Q9FXT4; F4MGX5; Q0IWR2; Q84UX2;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Alpha-galactosidase {ECO:0000303|PubMed:12423882};
DE            EC=3.2.1.22 {ECO:0000269|PubMed:12423882};
DE   AltName: Full=Alpha-D-galactoside galactohydrolase {ECO:0000305};
DE   AltName: Full=Melibiase {ECO:0000305};
DE   Flags: Precursor;
GN   OrderedLocusNames=Os10g0493600 {ECO:0000312|EMBL:BAT11449.1},
GN   LOC_Os10g35110 {ECO:0000312|EMBL:AAP54412.1};
GN   ORFNames=OSJNBa0041P03 {ECO:0000312|EMBL:AAM92832.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 56-95, FUNCTION, CATALYTIC
RP   ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC   STRAIN=cv. Nipponbare; TISSUE=Callus;
RX   PubMed=12423882; DOI=10.1016/s0031-9422(02)00368-0;
RA   Kim W.-D., Kobayashi O., Kaneko S., Sakakibara Y., Park G.-G., Kusakabe I.,
RA   Tanaka H., Kobayashi H.;
RT   "Alpha-galactosidase from cultured rice (Oryza sativa L. var. Nipponbare)
RT   cells.";
RL   Phytochemistry 61:621-630(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12791992; DOI=10.1126/science.1083523;
RA   Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA   Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA   Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA   Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA   Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA   Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA   Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA   Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA   Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA   Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA   Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA   Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA   Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA   Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA   Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA   Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA   Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT   "In-depth view of structure, activity, and evolution of rice chromosome
RT   10.";
RL   Science 300:1566-1569(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 101-284.
RC   STRAIN=cv. Tainung 67; TISSUE=Leaf;
RA   Lee R.H., Chen S.C.G.;
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 56-417 IN COMPLEX WITH
RP   ALPHA-D-GALACTOSE, ACTIVE SITES, AND DISULFIDE BONDS.
RX   PubMed=12657636; DOI=10.1074/jbc.m302292200;
RA   Fujimoto Z., Kaneko S., Momma M., Kobayashi H., Mizuno H.;
RT   "Crystal structure of rice alpha-galactosidase complexed with D-
RT   galactose.";
RL   J. Biol. Chem. 278:20313-20318(2003).
CC   -!- FUNCTION: Hydrolyzes melibiose, raffinose and stachyose in the
CC       following decreasing order of reactivity: raffinose, melibiose,
CC       stachyose (PubMed:12423882). Acts on both the terminal alpha-galactosyl
CC       residue and the side-chain alpha-galactosyl residue of the
CC       galactomanno-oligosaccharides (PubMed:12423882).
CC       {ECO:0000269|PubMed:12423882}.
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         Evidence={ECO:0000269|PubMed:12423882};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + melibiose = D-galactose + D-glucose;
CC         Xref=Rhea:RHEA:28663, ChEBI:CHEBI:4139, ChEBI:CHEBI:4167,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:28053;
CC         Evidence={ECO:0000269|PubMed:12423882};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28664;
CC         Evidence={ECO:0000269|PubMed:12423882};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + raffinose = D-galactose + sucrose; Xref=Rhea:RHEA:70275,
CC         ChEBI:CHEBI:4139, ChEBI:CHEBI:15377, ChEBI:CHEBI:16634,
CC         ChEBI:CHEBI:17992; Evidence={ECO:0000269|PubMed:12423882};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70276;
CC         Evidence={ECO:0000269|PubMed:12423882};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + stachyose = D-galactose + raffinose;
CC         Xref=Rhea:RHEA:70279, ChEBI:CHEBI:4139, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16634, ChEBI:CHEBI:17164;
CC         Evidence={ECO:0000269|PubMed:12423882};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70280;
CC         Evidence={ECO:0000269|PubMed:12423882};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-Gal-(1->6)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man +
CC         H2O = beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man + D-galactose;
CC         Xref=Rhea:RHEA:70339, ChEBI:CHEBI:4139, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:62785, ChEBI:CHEBI:189418;
CC         Evidence={ECO:0000269|PubMed:12423882};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70340;
CC         Evidence={ECO:0000269|PubMed:12423882};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-Man-(1->4)-[alpha-D-Gal-(1->6)]-beta-D-Man-(1->4)-beta-
CC         D-Man-(1->4)-D-Man + H2O = beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-
CC         D-Man-(1->4)-D-Man + D-galactose; Xref=Rhea:RHEA:70351,
CC         ChEBI:CHEBI:4139, ChEBI:CHEBI:15377, ChEBI:CHEBI:62973,
CC         ChEBI:CHEBI:189417; Evidence={ECO:0000269|PubMed:12423882};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70352;
CC         Evidence={ECO:0000269|PubMed:12423882};
CC   -!- ACTIVITY REGULATION: 1 mM Hg(2+) and Ag(2+) decrease activity by 98%
CC       and 96%, respectively. 1 mM Para-chloromercuribenzoic acid (PCMB)
CC       completely inhibits enzymatic activity. {ECO:0000269|PubMed:12423882}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.0. Slowly inactivated above pH 8.0 and below pH 3.
CC         {ECO:0000269|PubMed:12423882};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius with
CC         p-nitrophenyl-alpha-D-galactopyranoside as substrate.
CC         {ECO:0000269|PubMed:12423882};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
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DR   EMBL; AB039671; BAB12570.1; -; mRNA.
DR   EMBL; AC068950; AAM92832.1; -; Genomic_DNA.
DR   EMBL; DP000086; AAP54412.1; -; Genomic_DNA.
DR   EMBL; DP000086; ABB47819.1; -; Genomic_DNA.
DR   EMBL; AP008216; BAF26853.2; -; Genomic_DNA.
DR   EMBL; AP014966; BAT11449.1; -; Genomic_DNA.
DR   EMBL; AF251064; AAO85428.1; -; mRNA.
DR   RefSeq; XP_015613565.1; XM_015758079.1.
DR   RefSeq; XP_015613566.1; XM_015758080.1.
DR   PDB; 1UAS; X-ray; 1.50 A; A=56-417.
DR   PDBsum; 1UAS; -.
DR   AlphaFoldDB; Q9FXT4; -.
DR   SMR; Q9FXT4; -.
DR   IntAct; Q9FXT4; 9.
DR   STRING; 39947.Q9FXT4; -.
DR   ChEMBL; CHEMBL4537; -.
DR   CAZy; GH27; Glycoside Hydrolase Family 27.
DR   PaxDb; 39947-Q9FXT4; -.
DR   EnsemblPlants; Os10t0493600-01; Os10t0493600-01; Os10g0493600.
DR   GeneID; 4348988; -.
DR   Gramene; Os10t0493600-01; Os10t0493600-01; Os10g0493600.
DR   KEGG; osa:4348988; -.
DR   eggNOG; KOG2366; Eukaryota.
DR   InParanoid; Q9FXT4; -.
DR   OMA; YCGINEQ; -.
DR   OrthoDB; 1217107at2759; -.
DR   BRENDA; 3.2.1.22; 4460.
DR   EvolutionaryTrace; Q9FXT4; -.
DR   Proteomes; UP000000763; Chromosome 10.
DR   Proteomes; UP000059680; Chromosome 10.
DR   ExpressionAtlas; Q9FXT4; baseline and differential.
DR   GO; GO:0009505; C:plant-type cell wall; IBA:GO_Central.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IDA:UniProtKB.
DR   GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:RHEA.
DR   GO; GO:0051682; P:galactomannan catabolic process; IDA:UniProtKB.
DR   CDD; cd14792; GH27; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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:SF96; ALPHA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1.
DR   Pfam; PF16499; Melibiase_2; 1.
DR   Pfam; PF17801; Melibiase_C; 1.
DR   PRINTS; PR00740; GLHYDRLASE27.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
DR   Genevisible; Q9FXT4; OS.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Glycosidase;
KW   Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..55
FT                   /evidence="ECO:0000269|PubMed:12423882"
FT   CHAIN           56..417
FT                   /note="Alpha-galactosidase"
FT                   /id="PRO_0000001000"
FT   ACT_SITE        185
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:12657636"
FT   ACT_SITE        240
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000269|PubMed:12657636"
FT   BINDING         71
FT                   /ligand="alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:28061"
FT                   /evidence="ECO:0000269|PubMed:12657636"
FT   BINDING         106
FT                   /ligand="alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:28061"
FT                   /evidence="ECO:0000269|PubMed:12657636"
FT   BINDING         107
FT                   /ligand="alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:28061"
FT                   /evidence="ECO:0000269|PubMed:12657636"
FT   BINDING         156
FT                   /ligand="alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:28061"
FT                   /evidence="ECO:0000269|PubMed:12657636"
FT   BINDING         183
FT                   /ligand="alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:28061"
FT                   /evidence="ECO:0000269|PubMed:12657636"
FT   BINDING         185
FT                   /ligand="alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:28061"
FT                   /evidence="ECO:0000269|PubMed:12657636"
FT   BINDING         219
FT                   /ligand="alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:28061"
FT                   /evidence="ECO:0000269|PubMed:12657636"
FT   BINDING         236
FT                   /ligand="alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:28061"
FT                   /evidence="ECO:0000269|PubMed:12657636"
FT   BINDING         240
FT                   /ligand="alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:28061"
FT                   /evidence="ECO:0000269|PubMed:12657636"
FT   DISULFID        76..108
FT                   /evidence="ECO:0000269|PubMed:12657636"
FT   DISULFID        156..187
FT                   /evidence="ECO:0000269|PubMed:12657636"
FT   STRAND          66..70
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   HELIX           71..74
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   HELIX           80..92
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   HELIX           95..98
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   STRAND          102..104
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   TURN            124..126
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   HELIX           131..140
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   STRAND          144..154
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   STRAND          158..161
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   HELIX           167..177
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   STRAND          181..185
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   HELIX           194..208
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   STRAND          212..218
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   TURN            219..222
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   HELIX           224..226
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   HELIX           228..230
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   STRAND          233..236
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   HELIX           245..256
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   HELIX           257..261
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   STRAND          266..269
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   STRAND          277..280
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   HELIX           282..294
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   STRAND          299..301
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   HELIX           310..316
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   HELIX           319..325
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   STRAND          334..339
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   STRAND          342..348
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   STRAND          354..360
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   STRAND          362..364
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   STRAND          366..371
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   HELIX           372..374
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   STRAND          382..387
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   TURN            388..391
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   STRAND          392..404
FT                   /evidence="ECO:0007829|PDB:1UAS"
FT   STRAND          409..416
FT                   /evidence="ECO:0007829|PDB:1UAS"
SQ   SEQUENCE   417 AA;  45821 MW;  5F7B16326C042BF5 CRC64;
     MARASSSSSP PSPRLLLLLL VAVAATLLPE AAALGNFTAE SRGARWRSRR ARRRAFENGL
     GRTPQMGWNS WNHFYCGINE QIIRETADAL VNTGLAKLGY QYVNIDDCWA EYSRDSQGNF
     VPNRQTFPSG IKALADYVHA KGLKLGIYSD AGSQTCSNKM PGSLDHEEQD VKTFASWGVD
     YLKYDNCNDA GRSVMERYTR MSNAMKTYGK NIFFSLCEWG KENPATWAGR MGNSWRTTGD
     IADNWGSMTS RADENDQWAA YAGPGGWNDP DMLEVGNGGM SEAEYRSHFS IWALAKAPLL
     IGCDVRSMSQ QTKNILSNSE VIAVNQDSLG VQGKKVQSDN GLEVWAGPLS NNRKAVVLWN
     RQSYQATITA HWSNIGLAGS VAVTARDLWA HSSFAAQGQI SASVAPHDCK MYVLTPN
//