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O59893 (AXE2_PENPU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 59. 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:
Acetylxylan esterase 2

EC=3.1.1.72
Alternative name(s):
AXE II
Gene names
Name:axe-2
Synonyms:axeII
OrganismPenicillium purpurogenum (Soft rot fungus)
Taxonomic identifier1266744 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeTalaromyces

Protein attributes

Sequence length234 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone. Ref.2

Catalytic activity

Deacetylation of xylans and xylo-oligosaccharides.

Pathway

Glycan degradation; xylan degradation.

Subunit structure

Monomer.

Subcellular location

Secreted Ref.2.

Induction

Induced by xylan and repressed by glucose. Expressed at neutral pH, but not under alkaline or acidic condtions. Ref.3

Sequence similarities

Belongs to the cutinase family. Acetylxylan esterase subfamily.

Biophysicochemical properties

pH dependence:

Optimum pH is 6. Ref.2

Temperature dependence:

Optimum temperature is 60 degrees Celsius.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 2710
PRO_0000234624
Chain28 – 234207Acetylxylan esterase 2
PRO_0000234625

Sites

Active site1171 By similarity
Active site2021 By similarity
Active site2141 By similarity

Amino acid modifications

Glycosylation2071N-linked (GlcNAc...) Potential
Disulfide bond29 ↔ 106
Disulfide bond73 ↔ 79
Disulfide bond128 ↔ 188
Disulfide bond174 ↔ 206
Disulfide bond198 ↔ 205

Experimental info

Sequence conflict571L → I AA sequence Ref.2

Secondary structure

.................................. 234
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O59893 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: C033B3DA4E7BB6E1

FASTA23423,478
        10         20         30         40         50         60 
MHSKFFAASL LGLGAAAIPL EGVMEKRSCP AIHVFGARET TASPGYGSSS TVVNGVLSAY 

        70         80         90        100        110        120 
PGSTAEAINY PACGGQSSCG GASYSSSVAQ GIAAVASAVN SFNSQCPSTK IVLVGYSQGG 

       130        140        150        160        170        180 
EIMDVALCGG GDPNQGYTNT AVQLSSSAVN MVKAAIFMGD PMFRAGLSYE VGTCAAGGFD 

       190        200        210        220        230 
QRPAGFSCPS AAKIKSYCDA SDPYCCNGSN AATHQGYGSE YGSQALAFVK SKLG 

« Hide

References

[1]"Acetyl xylan esterase II from Penicillium purpurogenum is similar to an esterase from Trichoderma reesei but lacks a cellulose binding domain."
Gutierrez R., Cederlund E., Hjelmqvist L., Peirano A., Herrera F., Ghosh D., Duax W., Joernvall H., Eyzaguirre J.
FEBS Lett. 423:35-38(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 28-234.
[2]"Purification and characterization of two acetyl xylan esterases from Penicillium purpurogenum."
Egana L., Gutierrez R., Caputo V., Peirano A., Steiner J., Eyzaguirre J.
Biotechnol. Appl. Biochem. 24:33-39(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-57, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
[3]"The acetyl xylan esterase II gene from Penicillium purpurogenum is differentially expressed in several carbon sources, and tightly regulated by pH."
Chavez R., Schachter K., Navarro C., Peirano A., Bull P., Eyzaguirre J.
Biol. Res. 37:107-113(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[4]"Determination of a protein structure by iodination: the structure of iodinated acetylxylan esterase."
Ghosh D., Erman M., Sawicki M., Lala P., Weeks D.R., Li N., Pangborn W., Thiel D.J., Joernvall H., Gutierrez R., Eyzaguirre J.
Acta Crystallogr. D 55:779-784(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 28-234.
[5]"Multiple conformations of catalytic serine and histidine in acetylxylan esterase at 0.90 A."
Ghosh D., Sawicki M., Lala P., Erman M., Pangborn W., Eyzaguirre J., Gutierrez R., Joernvall H., Thiel D.J.
J. Biol. Chem. 276:11159-11166(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (0.9 ANGSTROMS) OF 28-234.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF015285 mRNA. Translation: AAC39371.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BS9X-ray1.10A28-234[»]
1G66X-ray0.90A28-234[»]
2AXEX-ray1.80A28-234[»]
ProteinModelPortalO59893.
SMRO59893. Positions 28-234.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

mycoCLAPAXE5B_PENPU.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16378.
BRENDA3.1.1.72. 4635.
UniPathwayUPA00114.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR000675. Cutinase.
[Graphical view]
PfamPF01083. Cutinase. 1 hit.
[Graphical view]
SUPFAMSSF53474. SSF53474. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO59893.

Entry information

Entry nameAXE2_PENPU
AccessionPrimary (citable) accession number: O59893
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: August 1, 1998
Last modified: June 11, 2014
This is version 59 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

PATHWAY comments

Index of metabolic and biosynthesis pathways