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P48842 (GANA_ASPAC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

EC=3.2.1.89
Alternative name(s):
Endo-1,4-beta-galactanase
Short name=Galactanase
Gene names
Name:gal1
OrganismAspergillus aculeatus
Taxonomic identifier5053 [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)

Catalytic activity

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

Post-translational modification

Glycosylated.

Sequence similarities

Belongs to the glycosyl hydrolase 53 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 4.0-4.5.

Temperature dependence:

Optimum temperature is 40-65 degrees Celsius.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.1
Chain17 – 350334Arabinogalactan endo-beta-1,4-galactanase
PRO_0000012221

Sites

Active site1521Proton donor By similarity
Active site2621Nucleophile By similarity

Amino acid modifications

Glycosylation1281N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis1981D → N: Broadens pH profile by 1 unit towards the basic end of the scale. Ref.2

Secondary structure

...................................................... 350
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P48842 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 9074249DFAB24CAC

FASTA35038,423
        10         20         30         40         50         60 
MFASLLLAAL PLLTHAALTY RGADISSLLL LEDEGYSYKN LNGQTQALET ILADAGINSI 

        70         80         90        100        110        120 
RQRVWVNPSD GSYDLDYNLE LAKRVKAAGM SLYLDLHLSD TWADPSDQTT PSGWSTTDLG 

       130        140        150        160        170        180 
TLKWQLYNYT LEVCNTFAEN DIDIEIISIG NEIRAGLLWP LGETSSYSNI GALLHSGAWG 

       190        200        210        220        230        240 
VKDSNLATTP KIMIHLDDGW SWDQQNYFYE TVLATGELLS TDFDYFGVSY YPFYSASATL 

       250        260        270        280        290        300 
ASLKTSLANL QSTYDKPVVV VETNWPVSCP NPAYAFPSDL SSIPFSVAGQ QEFLEKLAAV 

       310        320        330        340        350 
VEATTDGLGV YYWEPAWIGN AGLGSSCADN LMVDYTTDEV YESIETLGEL 

« Hide

References

[1]"Expression cloning, purification and characterization of a beta-1,4-galactanase from Aspergillus aculeatus."
Christgau S., Sandal T., Kofod L.V., Dalboege H.
Curr. Genet. 27:135-141(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-44.
Strain: KSM 510.
[2]"Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum."
Le Nours J., Ryttersgaard C., Lo Leggio L., Oestergaard P.R., Borchert T.V., Christensen L.L.H., Larsen S.
Protein Sci. 12:1195-1204(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-198.
[3]"Aspergillus aculeatus beta-1,4-galactanase: substrate recognition and relations to other glycoside hydrolases in clan GH-A."
Ryttersgaard C., Lo Leggio L., Coutinho P.M., Henrissat B., Larsen S.
Biochemistry 41:15135-15143(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L34599 mRNA. Translation: AAA32692.1.
PIRS51494.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FHLX-ray2.30A17-350[»]
1FOBX-ray1.80A17-350[»]
ProteinModelPortalP48842.
SMRP48842. Positions 17-350.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH53. Glycoside Hydrolase Family 53.
mycoCLAPGAN53A_ASPAC.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Other

EvolutionaryTraceP48842.

Entry information

Entry nameGANA_ASPAC
AccessionPrimary (citable) accession number: P48842
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 72 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries