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Q9FXT4 (AGAL_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-galactosidase

EC=3.2.1.22
Alternative name(s):
Alpha-D-galactoside galactohydrolase
Melibiase
Gene names
Ordered Locus Names:Os10g0493600, LOC_Os10g35110
ORF Names:OSJNBa0041P03
OrganismOryza sativa subsp. japonica (Rice) [Reference proteome]
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes melibiose, raffinose and stachyose in the following decreasing order of reactivity: raffinose, melibiose, stachyose. Ref.1

Catalytic activity

Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.

Enzyme regulation

1 mM Hg2+ and Ag2+ decrease activity by 98% and 96% respectively. 1 mM Para-chloromercuribenzoic acid (PCMB) completely inhibits enzymatic activity. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 27 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.0. Slowly inactivated above pH 8.0 and below pH 3. Ref.1

Temperature dependence:

Optimum temperature is 45 degrees Celsius with p-nitrophenyl-alpha-D-galactopyranoside as substrate.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 5555 Ref.1
Chain56 – 417362Alpha-galactosidase
PRO_0000001000

Regions

Region218 – 2225Substrate binding By similarity

Sites

Active site1851Nucleophile By similarity
Active site2401Proton donor By similarity

Amino acid modifications

Glycosylation361N-linked (GlcNAc...) Potential
Disulfide bond76 ↔ 108 By similarity
Disulfide bond156 ↔ 187 By similarity

Secondary structure

................................................................. 417
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9FXT4 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 5F7B16326C042BF5

FASTA41745,821
        10         20         30         40         50         60 
MARASSSSSP PSPRLLLLLL VAVAATLLPE AAALGNFTAE SRGARWRSRR ARRRAFENGL 

        70         80         90        100        110        120 
GRTPQMGWNS WNHFYCGINE QIIRETADAL VNTGLAKLGY QYVNIDDCWA EYSRDSQGNF 

       130        140        150        160        170        180 
VPNRQTFPSG IKALADYVHA KGLKLGIYSD AGSQTCSNKM PGSLDHEEQD VKTFASWGVD 

       190        200        210        220        230        240 
YLKYDNCNDA GRSVMERYTR MSNAMKTYGK NIFFSLCEWG KENPATWAGR MGNSWRTTGD 

       250        260        270        280        290        300 
IADNWGSMTS RADENDQWAA YAGPGGWNDP DMLEVGNGGM SEAEYRSHFS IWALAKAPLL 

       310        320        330        340        350        360 
IGCDVRSMSQ QTKNILSNSE VIAVNQDSLG VQGKKVQSDN GLEVWAGPLS NNRKAVVLWN 

       370        380        390        400        410 
RQSYQATITA HWSNIGLAGS VAVTARDLWA HSSFAAQGQI SASVAPHDCK MYVLTPN 

« Hide

References

« Hide 'large scale' references
[1]"Alpha-galactosidase from cultured rice (Oryza sativa L. var. Nipponbare) cells."
Kim W.-D., Kobayashi O., Kaneko S., Sakakibara Y., Park G.-G., Kusakabe I., Tanaka H., Kobayashi H.
Phytochemistry 61:621-630(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 56-95, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
Strain: cv. Nipponbare.
Tissue: Callus.
[2]"In-depth view of structure, activity, and evolution of rice chromosome 10."
Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S., Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D., Oates R., Palmer M., Pries G., Gibson J., Anderson H. expand/collapse author list , Paradkar M., Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F., Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M., Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R., Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F., Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D., Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R., Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K., Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S., Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S., Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R., Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M., Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R., Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E., Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.
Science 300:1566-1569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[3]"The map-based sequence of the rice genome."
International rice genome sequencing project (IRGSP)
Nature 436:793-800(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[4]"The rice annotation project database (RAP-DB): 2008 update."
The rice annotation project (RAP)
Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: cv. Nipponbare.
[5]Lee R.H., Chen S.C.G.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 101-284.
Strain: cv. Tainung 67.
Tissue: Leaf.
[6]"Crystal structure of rice alpha-galactosidase complexed with D-galactose."
Fujimoto Z., Kaneko S., Momma M., Kobayashi H., Mizuno H.
J. Biol. Chem. 278:20313-20318(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 56-417 IN COMPLEX WITH D-GALACTOSE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB039671 mRNA. Translation: BAB12570.1.
AC068950 Genomic DNA. Translation: AAM92832.1.
DP000086 Genomic DNA. Translation: AAP54412.1.
AP008216 Genomic DNA. Translation: BAF26853.2.
AF251064 mRNA. Translation: AAO85428.1.
RefSeqNP_001064939.2. NM_001071474.2.
UniGeneOs.88093.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UASX-ray1.50A56-417[»]
ProteinModelPortalQ9FXT4.
SMRQ9FXT4. Positions 56-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9FXT4. 9 interactions.
STRING39947.LOC_Os10g35110.2.

Chemistry

ChEMBLCHEMBL4537.

Protein family/group databases

CAZyGH27. Glycoside Hydrolase Family 27.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsOS10T0493600-01; OS10T0493600-01; OS10G0493600.
GeneID4348988.
KEGGosa:4348988.

Organism-specific databases

GrameneQ9FXT4.

Phylogenomic databases

eggNOGNOG68897.
KOK07407.
OMARSVMERY.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR013780. Glyco_hydro_13_b.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_GHD.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02065. Melibiase. 1 hit.
[Graphical view]
PRINTSPR00740. GLHYDRLASE27.
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9FXT4.

Entry information

Entry nameAGAL_ORYSJ
AccessionPrimary (citable) accession number: Q9FXT4
Secondary accession number(s): Q0IWR2, Q84UX2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2001
Last modified: May 14, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries