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Q9FXT4

- AGAL_ORYSJ

UniProt

Q9FXT4 - AGAL_ORYSJ

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Protein
Alpha-galactosidase
Gene
Os10g0493600, LOC_Os10g35110, OSJNBa0041P03
Organism
Oryza sativa subsp. japonica (Rice)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Enzyme regulationi

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

pH dependencei

Optimum pH is 5.0. Slowly inactivated above pH 8.0 and below pH 3.1 Publication

Temperature dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei185 – 1851Nucleophile By similarity
Active sitei240 – 2401Proton donor By similarity

GO - Molecular functioni

  1. raffinose alpha-galactosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. leaf morphogenesis Source: EnsemblPlants/Gramene
  3. positive regulation of flower development Source: EnsemblPlants/Gramene
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH27. Glycoside Hydrolase Family 27.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-galactosidase (EC:3.2.1.22)
Alternative name(s):
Alpha-D-galactoside galactohydrolase
Melibiase
Gene namesi
Ordered Locus Names:Os10g0493600, LOC_Os10g35110
ORF Names:OSJNBa0041P03
OrganismiOryza sativa subsp. japonica (Rice)
Taxonomic identifieri39947 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza
ProteomesiUP000000763: Chromosome 10

Organism-specific databases

GrameneiQ9FXT4.

Subcellular locationi

GO - Cellular componenti

  1. plant-type cell wall Source: RefGenome
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 55551 Publication
Add
BLAST
Chaini56 – 417362Alpha-galactosidase
PRO_0000001000Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi36 – 361N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi76 ↔ 108 By similarity
Disulfide bondi156 ↔ 187 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Protein-protein interaction databases

IntActiQ9FXT4. 9 interactions.
STRINGi39947.LOC_Os10g35110.2.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi66 – 705
Helixi71 – 744
Helixi80 – 9213
Helixi95 – 984
Beta strandi102 – 1043
Turni124 – 1263
Helixi131 – 14010
Beta strandi144 – 15411
Beta strandi158 – 1614
Helixi167 – 17711
Beta strandi181 – 1855
Helixi194 – 20815
Beta strandi212 – 2187
Turni219 – 2224
Helixi224 – 2263
Helixi228 – 2303
Beta strandi233 – 2364
Helixi245 – 25612
Helixi257 – 2615
Beta strandi266 – 2694
Beta strandi277 – 2804
Helixi282 – 29413
Beta strandi299 – 3013
Helixi310 – 3167
Helixi319 – 3257
Beta strandi334 – 3396
Beta strandi342 – 3487
Beta strandi354 – 3607
Beta strandi362 – 3643
Beta strandi366 – 3716
Helixi372 – 3743
Beta strandi382 – 3876
Turni388 – 3914
Beta strandi392 – 40413
Beta strandi409 – 4168

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UASX-ray1.50A56-417[»]
ProteinModelPortaliQ9FXT4.
SMRiQ9FXT4. Positions 56-417.

Miscellaneous databases

EvolutionaryTraceiQ9FXT4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni218 – 2225Substrate binding By similarity

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG68897.
KOiK07407.
OMAiRSVMERY.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR013780. Glyco_hydro_13_b.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_GHD.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02065. Melibiase. 1 hit.
[Graphical view]
PRINTSiPR00740. GLHYDRLASE27.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9FXT4-1 [UniParc]FASTAAdd to Basket

« Hide

MARASSSSSP PSPRLLLLLL VAVAATLLPE AAALGNFTAE SRGARWRSRR    50
ARRRAFENGL GRTPQMGWNS WNHFYCGINE QIIRETADAL VNTGLAKLGY 100
QYVNIDDCWA EYSRDSQGNF VPNRQTFPSG IKALADYVHA KGLKLGIYSD 150
AGSQTCSNKM PGSLDHEEQD VKTFASWGVD YLKYDNCNDA GRSVMERYTR 200
MSNAMKTYGK NIFFSLCEWG KENPATWAGR MGNSWRTTGD IADNWGSMTS 250
RADENDQWAA YAGPGGWNDP DMLEVGNGGM SEAEYRSHFS IWALAKAPLL 300
IGCDVRSMSQ QTKNILSNSE VIAVNQDSLG VQGKKVQSDN GLEVWAGPLS 350
NNRKAVVLWN RQSYQATITA HWSNIGLAGS VAVTARDLWA HSSFAAQGQI 400
SASVAPHDCK MYVLTPN 417
Length:417
Mass (Da):45,821
Last modified:March 1, 2001 - v1
Checksum:i5F7B16326C042BF5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqiNP_001064939.2. NM_001071474.2.
UniGeneiOs.88093.

Genome annotation databases

EnsemblPlantsiOS10T0493600-01; OS10T0493600-01; OS10G0493600.
GeneIDi4348988.
KEGGiosa:4348988.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
RefSeqi NP_001064939.2. NM_001071474.2.
UniGenei Os.88093.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UAS X-ray 1.50 A 56-417 [» ]
ProteinModelPortali Q9FXT4.
SMRi Q9FXT4. Positions 56-417.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9FXT4. 9 interactions.
STRINGi 39947.LOC_Os10g35110.2.

Chemistry

ChEMBLi CHEMBL4537.

Protein family/group databases

CAZyi GH27. Glycoside Hydrolase Family 27.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi OS10T0493600-01 ; OS10T0493600-01 ; OS10G0493600 .
GeneIDi 4348988.
KEGGi osa:4348988.

Organism-specific databases

Gramenei Q9FXT4.

Phylogenomic databases

eggNOGi NOG68897.
KOi K07407.
OMAi RSVMERY.

Miscellaneous databases

EvolutionaryTracei Q9FXT4.

Family and domain databases

Gene3Di 2.60.40.1180. 1 hit.
3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR013780. Glyco_hydro_13_b.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_GHD.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF02065. Melibiase. 1 hit.
[Graphical view ]
PRINTSi PR00740. GLHYDRLASE27.
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiAGAL_ORYSJ
AccessioniPrimary (citable) accession number: Q9FXT4
Secondary accession number(s): Q0IWR2, Q84UX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2001
Last modified: September 3, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Oryza sativa (rice)
    Index of Oryza sativa entries and their corresponding gene designations
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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