GenomeNet

Database: UniProt
Entry: Q9FXT4
LinkDB: Q9FXT4
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   26-NOV-2014, 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;
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   InParanoid; Q9FXT4; -.
DR   KO; K07407; -.
DR   OMA; RSVMERY; -.
DR   Reactome; REACT_225825; Glycosphingolipid metabolism.
DR   EvolutionaryTrace; Q9FXT4; -.
DR   ExpressionAtlas; Q9FXT4; baseline.
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:0009965; P:leaf morphogenesis; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0000023; P:maltose metabolic process; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0007020; P:microtubule nucleation; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0043085; P:positive regulation of catalytic activity; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0009911; P:positive regulation of flower development; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0019252; P:starch biosynthetic process; 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       {ECO:0000244|PDB:1UAS}.
FT   HELIX        71     74       {ECO:0000244|PDB:1UAS}.
FT   HELIX        80     92       {ECO:0000244|PDB:1UAS}.
FT   HELIX        95     98       {ECO:0000244|PDB:1UAS}.
FT   STRAND      102    104       {ECO:0000244|PDB:1UAS}.
FT   TURN        124    126       {ECO:0000244|PDB:1UAS}.
FT   HELIX       131    140       {ECO:0000244|PDB:1UAS}.
FT   STRAND      144    154       {ECO:0000244|PDB:1UAS}.
FT   STRAND      158    161       {ECO:0000244|PDB:1UAS}.
FT   HELIX       167    177       {ECO:0000244|PDB:1UAS}.
FT   STRAND      181    185       {ECO:0000244|PDB:1UAS}.
FT   HELIX       194    208       {ECO:0000244|PDB:1UAS}.
FT   STRAND      212    218       {ECO:0000244|PDB:1UAS}.
FT   TURN        219    222       {ECO:0000244|PDB:1UAS}.
FT   HELIX       224    226       {ECO:0000244|PDB:1UAS}.
FT   HELIX       228    230       {ECO:0000244|PDB:1UAS}.
FT   STRAND      233    236       {ECO:0000244|PDB:1UAS}.
FT   HELIX       245    256       {ECO:0000244|PDB:1UAS}.
FT   HELIX       257    261       {ECO:0000244|PDB:1UAS}.
FT   STRAND      266    269       {ECO:0000244|PDB:1UAS}.
FT   STRAND      277    280       {ECO:0000244|PDB:1UAS}.
FT   HELIX       282    294       {ECO:0000244|PDB:1UAS}.
FT   STRAND      299    301       {ECO:0000244|PDB:1UAS}.
FT   HELIX       310    316       {ECO:0000244|PDB:1UAS}.
FT   HELIX       319    325       {ECO:0000244|PDB:1UAS}.
FT   STRAND      334    339       {ECO:0000244|PDB:1UAS}.
FT   STRAND      342    348       {ECO:0000244|PDB:1UAS}.
FT   STRAND      354    360       {ECO:0000244|PDB:1UAS}.
FT   STRAND      362    364       {ECO:0000244|PDB:1UAS}.
FT   STRAND      366    371       {ECO:0000244|PDB:1UAS}.
FT   HELIX       372    374       {ECO:0000244|PDB:1UAS}.
FT   STRAND      382    387       {ECO:0000244|PDB:1UAS}.
FT   TURN        388    391       {ECO:0000244|PDB:1UAS}.
FT   STRAND      392    404       {ECO:0000244|PDB:1UAS}.
FT   STRAND      409    416       {ECO:0000244|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
//
DBGET integrated database retrieval system