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Q8X168 (GANA_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 44. 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:
Arabinogalactan endo-beta-1,4-galactanase A

EC=3.2.1.89
Alternative name(s):
Endo-1,4-beta-galactanase A
Short name=Galactanase A
Gene names
Name:galA
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endogalactanase involved in the degradation of plant cell wall polysaccharides, and more particularly of hairy regions of pectin By similarity. Ref.1

Catalytic activity

The enzyme specifically hydrolyzes (1->4)-beta-D-galactosidic linkages in type I arabinogalactans.

Subcellular location

Secreted Ref.1.

Induction

Specifically expressed on arabinose and galacturonic acid. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 53 family.

Biophysicochemical properties

pH dependence:

Optimum pH is between 4.0 and 4.5. Ref.1

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cell wall biogenesis/degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological_processpectin catabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionarabinogalactan endo-1,4-beta-galactosidase activity

Inferred from direct assay Ref.1. Source: UniProtKB

glucosidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 350334Arabinogalactan endo-beta-1,4-galactanase A
PRO_0000394947

Sites

Active site1521Proton donor By similarity
Active site2621Nucleophile By similarity

Amino acid modifications

Glycosylation1281N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q8X168 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 3353286DECB85DD6

FASTA35038,734
        10         20         30         40         50         60 
MIYPLLLSAL PLLSSAALTY RGADISSLLI EEDAGISYKN LNGETQALED ILVNNGVNSI 

        70         80         90        100        110        120 
RQRVWVDPSD GSYDLDYNLK LAKRVQAAGM SIYLDLHLSD TWADPSDQTT PTGWSTTDID 

       130        140        150        160        170        180 
TLTWQLYNYT LDVCNTFAEN DIDIEIVSIG NEISSGLLWP LGKTSNYDNI AKLLHSGAWG 

       190        200        210        220        230        240 
VKDSNQATTP KIMIHLDNGW DWEEQEYFYK TVLATGSLLS TDFDLMGVSY YPFYNSEATL 

       250        260        270        280        290        300 
SALQTSLTNM QSNYDKSVVV VETNWPVSCP DPEYSFPSDL SSIPFSAAGQ EEFLEKLAEV 

       310        320        330        340        350 
VEGVTDGLGI YYWEPAWVDN AALGSSCADN LMVDIDTDEV LESVTVFEDL 

« Hide

References

[1]"Endogalactanase A from Aspergillus niger is specifically induced on L-arabinose and galacturonic acid and plays an important role in the degradation of pectic hairy regions."
de Vries R.P., Paenicova L., Hinz S., Kester H.C.M., Benen J.A.E., Beldman G.A., Visser J.
Eur. J. Biochem. 269:4985-4993(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, SUBCELLULAR LOCATION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ305303 Genomic DNA. Translation: CAC83735.1.

3D structure databases

ProteinModelPortalQ8X168.
SMRQ8X168. Positions 17-350.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH53. Glycoside Hydrolase Family 53.
mycoCLAPGAN53A_ASPNG.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG3867.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR011683. Glyco_hydro_53.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF07745. Glyco_hydro_53. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGANA_ASPNG
AccessionPrimary (citable) accession number: Q8X168
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: March 1, 2002
Last modified: June 11, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries