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Database: UniProt
Entry: Q9FXT4
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Original site: Q9FXT4 
ID   AGAL_ORYSJ              Reviewed;         417 AA.
AC   Q9FXT4; Q0IWR2; Q84UX2;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   01-OCT-2014, entry version 89.
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;
GN   OrderedLocusNames=Os10g0493600, LOC_Os10g35110;
GN   ORFNames=OSJNBa0041P03;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Ehrhartoideae; Oryzeae; Oryza.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 56-95, FUNCTION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME 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.,
RA   Kusakabe I., Tanaka H., Kobayashi H.;
RT   "Alpha-galactosidase from cultured rice (Oryza sativa L. var.
RT   Nipponbare) 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.,
RA   Thompson S., Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S.,
RA   Henry D., Oates R., Palmer M., Pries G., Gibson J., Anderson H.,
RA   Paradkar M., Crane L., Dale J., Carver M.B., Wood T., Frisch D.,
RA   Engler F., Soderlund C., Palmer L.E., Teytelman L., Nascimento L.,
RA   De la Bastide M., Spiegel L., Ware D., O'Shaughnessy A., Dike S.,
RA   Dedhia N., Preston R., Huang E., Ferraro K., Kuit K., Miller B.,
RA   Zutavern T., Katzenberger F., Muller S., Balija V., Martienssen R.A.,
RA   Stein L., Minx P., Johnson D., Cordum H., Mardis E., Cheng Z.,
RA   Jiang J., Wilson R., McCombie W.R., Wing R.A., Yuan Q., Ouyang S.,
RA   Liu J., Jones K.M., Gansberger K., Moffat K., Hill J., Tsitrin T.,
RA   Overton L., Bera J., Kim M., Jin S., Tallon L., Ciecko A., Pai G.,
RA   Van Aken S., Utterback T., Reidmuller S., Bormann J., Feldblyum T.,
RA   Hsiao J., Zismann V., Blunt S., de Vazeille A.R., Shaffer T., Koo H.,
RA   Suh B., Yang Q., Haas B., Peterson J., Pertea M., Volfovsky N.,
RA   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.,
RA   Bowers J.E., Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT   "In-depth view of structure, activity, and evolution of rice
RT   chromosome 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   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   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 56-417 IN COMPLEX WITH
RP   D-GALACTOSE.
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. {ECO:0000269|PubMed:12423882}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing alpha-D-
CC       galactose residues in alpha-D-galactosides, including galactose
CC       oligosaccharides, galactomannans and galactolipids.
CC   -!- ENZYME 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.
CC       {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
CC         3. {ECO:0000269|PubMed:12423882};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius with p-nitrophenyl-
CC         alpha-D-galactopyranoside as substrate.
CC         {ECO:0000269|PubMed:12423882};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family.
CC       {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; AP008216; BAF26853.2; -; Genomic_DNA.
DR   EMBL; AF251064; AAO85428.1; -; mRNA.
DR   RefSeq; NP_001064939.2; NM_001071474.2.
DR   UniGene; Os.88093; -.
DR   PDB; 1UAS; X-ray; 1.50 A; A=56-417.
DR   PDBsum; 1UAS; -.
DR   ProteinModelPortal; Q9FXT4; -.
DR   SMR; Q9FXT4; 56-417.
DR   IntAct; Q9FXT4; 9.
DR   STRING; 39947.LOC_Os10g35110.2; -.
DR   ChEMBL; CHEMBL4537; -.
DR   CAZy; GH27; Glycoside Hydrolase Family 27.
DR   EnsemblPlants; OS10T0493600-01; OS10T0493600-01; OS10G0493600.
DR   GeneID; 4348988; -.
DR   KEGG; osa:4348988; -.
DR   Gramene; Q9FXT4; -.
DR   eggNOG; NOG68897; -.
DR   KO; K07407; -.
DR   OMA; RSVMERY; -.
DR   EvolutionaryTrace; Q9FXT4; -.
DR   GO; GO:0009505; C:plant-type cell wall; IBA:RefGenome.
DR   GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0009965; P:leaf morphogenesis; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0009911; P:positive regulation of flower development; IEA:EnsemblPlants/Gramene.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR013780; Glyco_hydro_13_b.
DR   InterPro; IPR002241; Glyco_hydro_27.
DR   InterPro; IPR000111; Glyco_hydro_GHD.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF02065; Melibiase; 1.
DR   PRINTS; PR00740; GLHYDRLASE27.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Signal.
FT   SIGNAL        1     55       {ECO:0000269|PubMed:12423882}.
FT   CHAIN        56    417       Alpha-galactosidase.
FT                                /FTId=PRO_0000001000.
FT   REGION      218    222       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    185    185       Nucleophile. {ECO:0000250}.
FT   ACT_SITE    240    240       Proton donor. {ECO:0000250}.
FT   CARBOHYD     36     36       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     76    108       {ECO:0000250}.
FT   DISULFID    156    187       {ECO:0000250}.
FT   STRAND       66     70
FT   HELIX        71     74
FT   HELIX        80     92
FT   HELIX        95     98
FT   STRAND      102    104
FT   TURN        124    126
FT   HELIX       131    140
FT   STRAND      144    154
FT   STRAND      158    161
FT   HELIX       167    177
FT   STRAND      181    185
FT   HELIX       194    208
FT   STRAND      212    218
FT   TURN        219    222
FT   HELIX       224    226
FT   HELIX       228    230
FT   STRAND      233    236
FT   HELIX       245    256
FT   HELIX       257    261
FT   STRAND      266    269
FT   STRAND      277    280
FT   HELIX       282    294
FT   STRAND      299    301
FT   HELIX       310    316
FT   HELIX       319    325
FT   STRAND      334    339
FT   STRAND      342    348
FT   STRAND      354    360
FT   STRAND      362    364
FT   STRAND      366    371
FT   HELIX       372    374
FT   STRAND      382    387
FT   TURN        388    391
FT   STRAND      392    404
FT   STRAND      409    416
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
//
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