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Reviewed, UniProtKB/Swiss-Prot P28351 (AGAL_ASPNG)

Last modified June 16, 2009. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alpha-galactosidase A
    EC=3.2.1.22
Alternative name(s):
    Melibiase
Gene names
Name: aglA
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaeAspergillus

Protein attributes

Sequence length545 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Represents a minor extracellular alpha-galactosidase activity in A.niger.

Catalytic activity

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

Subcellular location

Secreted.

Post-translational modification

A C-terminal Ser/Thr-rich region may provide possible sites for O-glycosylation.

Sequence similarities

Belongs to the glycosyl hydrolase 27 family.

Contains 1 ricin B-type lectin domain.

Caution

It is uncertain whether Met-1 or Met-9 is the initiator.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandLectin
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalpha-galactosidase activity

Inferred from electronic annotation. Source: EC

sugar binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Ref.1
Chain32 – 545514Alpha-galactosidase A
PRO_0000000999

Regions

Domain421 – 51898Ricin B-type lectin

Sites

Active site1621Nucleophile By similarity
Active site2201Proton donor By similarity

Amino acid modifications

Glycosylation571N-linked (GlcNAc...) Potential
Glycosylation951N-linked (GlcNAc...) Potential
Glycosylation1011N-linked (GlcNAc...) Potential
Glycosylation1311N-linked (GlcNAc...) Potential
Glycosylation2111N-linked (GlcNAc...) Potential
Glycosylation3631N-linked (GlcNAc...) Potential
Glycosylation4441N-linked (GlcNAc...) Potential
Disulfide bond54 ↔ 86 By similarity
Disulfide bond134 ↔ 164 By similarity

Sequences

Sequence LengthMass (Da)Tools
P28351-1 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 2DC5A710CE95D59C

FASTA54560,148
        10         20         30         40         50         60 
MIQGLESIMN QGTKRILLAA TLAATPWQVY GSIEQPSLLP TPPMGFNNWA RFMCDLNETL 

        70         80         90        100        110        120 
FTETADTMAA NGLRDAGYNR INLDDCWMAY QRSDNGSLQW NTTKFPHGLP WLAKYVKAKG 

       130        140        150        160        170        180 
FHFGIYEDSG NMTCGGYPGS YNHEEQDANT FASWGIDYLK LDGCNVYATQ GRTLEEEYKQ 

       190        200        210        220        230        240 
RYGHWHQVLS KMQHPLIFSE SAPAYFAGTD NNTDWYTVMD WVPIYGELAR HSTDILVYSG 

       250        260        270        280        290        300 
AGSAWDSIMN NYNYNTLLAR YQRPGYFNDP DFLIPDHPGL TADEKRSHFA LWASFSAPLI 

       310        320        330        340        350        360 
ISAYIPALSK DEIAFLTNEA LIAVNQDPLA QQATLASRDD TLDILTRSLA NGDRLLTVLN 

       370        380        390        400        410        420 
KGNTTVTRDI PVQWLGLTET DCTYTAEDLW DGKTQKISDH IKIELASHAT AVFRLSLPQG 

       430        440        450        460        470        480 
CSSVVPTGLV FNTASGNCLT AASNSSVAFQ SCNGETSQIW QVTPSGVIRP VSQTTQCLAA 

       490        500        510        520        530        540 
DGNLVKLQAC DSTDSDGQKW TYPVTGNLKN AKTDGCLTEG SVQMKSCLYE RDGQVFGLPS 


GVQLA 

« Hide

References

[1]"Cloning and expression of a member of the Aspergillus niger gene family encoding alpha-galactosidase."
den Herder I.F., Rosell A.M.M., van Zuilen C.M., Punt P.J., van den Hondel C.A.M.J.J.
Mol. Gen. Genet. 233:404-410(1992) [PubMed: 1320186] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 32-59.
Strain: ATCC 9089 / N402.

Cross-references

Sequence databases

X63348 Genomic DNA. Translation: CAA44950.1.
PIRS23582.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
GH27. Glycoside Hydrolase Family 27.

PTM databases

GlycoSuiteDBP28351.

Enzyme and pathway databases

BRENDA3.2.1.22. 277.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_GHD.
IPR000772. Ricin_B_lectin.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PfamPF02065. Melibiase. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
PRINTSPR00740. GLHYDRLASE27.
ProDomPD002572. Glyco_hydro_GHD. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
PROSITEPS00512. ALPHA_GALACTOSIDASE. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAGAL_ASPNG
AccessionPrimary (citable) accession number: P28351
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents