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P14749 (AGAL_CYATE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 27, 2011. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismCyamopsis tetragonoloba (Guar) (Cluster bean)
Taxonomic identifier3832 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsfabidsFabalesFabaceaePapilionoideaeIndigofereaeCyamopsis

Protein attributes

Sequence length411 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the hydrolysis of the galactomannan, it splits alpha-linked galactose moieties. It is particularly suitable for the hydrolysis of guar gum to a gum with improved gelling properties. Preferentially cleaves alpha-1,6 glycoside linkages.

Catalytic activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 27 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424
Propeptide25 – 4723
PRO_0000001002
Chain48 – 411364Alpha-galactosidase
PRO_0000001003

Regions

Region210 – 2145Substrate binding By similarity

Sites

Active site1771Nucleophile By similarity
Active site2321Proton donor By similarity

Amino acid modifications

Glycosylation321N-linked (GlcNAc...) Potential
Glycosylation1451N-linked (GlcNAc...) Potential
Glycosylation3521N-linked (GlcNAc...) Potential
Disulfide bond68 ↔ 100 By similarity
Disulfide bond148 ↔ 179 By similarity

Sequences

Sequence LengthMass (Da)Tools
P14749 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 5B1715858D1AB11E

FASTA41145,136
        10         20         30         40         50         60 
MATHYSIIGG MIIVVLLMII GSEGGRLLEK KNRTSAEAEH YNVRRYLAEN GLGQTPPMGW 

        70         80         90        100        110        120 
NSWNHFGCDI NENVVRETAD AMVSTGLAAL GYQYINLDDC WAELNRDSEG NMVPNAAAFP 

       130        140        150        160        170        180 
SGIKALADYV HSKGLKLGVY SDAGNQTCSK RMPGSLGHEE QDAKTFASWG VDYLKYDNCE 

       190        200        210        220        230        240 
NLGISVKERY PPMGKALLSS GRPIFFSMCE WGWEDPQIWA KSIGNSWRTT GDIEDNWNSM 

       250        260        270        280        290        300 
TSIADSNDKW ASYAGPGGWN DPDMLEVGNG GMTTEEYRSH FSIWALAKAP LLVGCDIRAM 

       310        320        330        340        350        360 
DDTTHELISN AEVIAVNQDK LGVQGKKVKS TNDLEVWAGP LSDNKVAVIL WNRSSSRATV 

       370        380        390        400        410 
TASWSDIGLQ QGTTVDARDL WEHSTQSLVS GEISAEIDSH ACKMYVLTPR S 

« Hide

References

[1]"Cloning and nucleotide sequence of the alpha-galactosidase cDNA from Cyamopsis tetragonoloba (guar)."
Overbeeke N., Fellinger A.J., Toonen M.Y., van Wassenaar D., Verrips C.T.
Plant Mol. Biol. 13:541-550(1989) [PubMed: 2577496] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Aleurone.
[2]"Messenger RNA from isolated aleurone cells directs the synthesis of an alpha-galactosidase found in the endosperm during germination of guar (Cyamopsis tetragonaloba) seed."
Hughes S.G., Overbeeke N., Robinson S., Pollock K., Smeets F.L.M.
Plant Mol. Biol. 11:783-789(1988) [Agricola: IND91035194]
Cited for: PROTEIN SEQUENCE OF 48-57 AND 172-178.
Tissue: Seed.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14619 mRNA. Translation: CAA32772.1.
PIRS07472.

3D structure databases

ProteinModelPortalP14749.
SMRP14749. Positions 49-409.
ModBaseSearch...

Protein family/group databases

CAZyGH27. Glycoside Hydrolase Family 27.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR013780. Glyco_hydro_13_b.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_GHD.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
PfamPF02065. Melibiase. 1 hit.
[Graphical view]
PRINTSPR00740. GLHYDRLASE27.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAGAL_CYATE
AccessionPrimary (citable) accession number: P14749
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 27, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families