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Protein

Acetylxylan esterase 2

Gene

axe-2

Organism
Penicillium purpurogenum (Soft rot fungus) (Talaromyces purpurogenus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone.1 Publication

Catalytic activityi

Deacetylation of xylans and xylo-oligosaccharides.

pH dependencei

Optimum pH is 6.1 Publication

Temperature dependencei

Optimum temperature is 60 degrees Celsius.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei117 – 1171By similarity
Active sitei202 – 2021By similarity
Active sitei214 – 2141By similarity

GO - Molecular functioni

  1. acetylxylan esterase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
  2. xylan catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16378.
UniPathwayiUPA00114.

Protein family/group databases

mycoCLAPiAXE5B_PENPU.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylxylan esterase 2 (EC:3.1.1.72)
Alternative name(s):
AXE II
Gene namesi
Name:axe-2
Synonyms:axeII
OrganismiPenicillium purpurogenum (Soft rot fungus) (Talaromyces purpurogenus)
Taxonomic identifieri1266744 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeTalaromyces

Subcellular locationi

  1. Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Propeptidei18 – 27102 PublicationsPRO_0000234624
Chaini28 – 234207Acetylxylan esterase 2PRO_0000234625Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 106
Disulfide bondi73 ↔ 79
Disulfide bondi128 ↔ 188
Disulfide bondi174 ↔ 206
Disulfide bondi198 ↔ 205
Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Expressioni

Inductioni

Induced by xylan and repressed by glucose. Expressed at neutral pH, but not under alkaline or acidic condtions.1 Publication

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
234
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 377Combined sources
Helixi47 – 493Combined sources
Helixi50 – 5910Combined sources
Beta strandi64 – 674Combined sources
Helixi77 – 793Combined sources
Helixi84 – 10522Combined sources
Beta strandi110 – 1167Combined sources
Helixi118 – 12811Combined sources
Helixi133 – 1353Combined sources
Helixi146 – 1516Combined sources
Beta strandi152 – 1598Combined sources
Beta strandi170 – 1734Combined sources
Beta strandi175 – 1773Combined sources
Helixi191 – 1933Combined sources
Beta strandi194 – 1974Combined sources
Turni203 – 2053Combined sources
Helixi212 – 2154Combined sources
Helixi217 – 23317Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BS9X-ray1.10A28-234[»]
1G66X-ray0.90A28-234[»]
2AXEX-ray1.80A28-234[»]
ProteinModelPortaliO59893.
SMRiO59893. Positions 28-234.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO59893.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000675. Cutinase.
[Graphical view]
PfamiPF01083. Cutinase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O59893-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHSKFFAASL LGLGAAAIPL EGVMEKRSCP AIHVFGARET TASPGYGSSS
60 70 80 90 100
TVVNGVLSAY PGSTAEAINY PACGGQSSCG GASYSSSVAQ GIAAVASAVN
110 120 130 140 150
SFNSQCPSTK IVLVGYSQGG EIMDVALCGG GDPNQGYTNT AVQLSSSAVN
160 170 180 190 200
MVKAAIFMGD PMFRAGLSYE VGTCAAGGFD QRPAGFSCPS AAKIKSYCDA
210 220 230
SDPYCCNGSN AATHQGYGSE YGSQALAFVK SKLG
Length:234
Mass (Da):23,478
Last modified:August 1, 1998 - v1
Checksum:iC033B3DA4E7BB6E1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti57 – 571L → I AA sequence (PubMed:8756392).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF015285 mRNA. Translation: AAC39371.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF015285 mRNA. Translation: AAC39371.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BS9X-ray1.10A28-234[»]
1G66X-ray0.90A28-234[»]
2AXEX-ray1.80A28-234[»]
ProteinModelPortaliO59893.
SMRiO59893. Positions 28-234.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

mycoCLAPiAXE5B_PENPU.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.
BioCyciMetaCyc:MONOMER-16378.

Miscellaneous databases

EvolutionaryTraceiO59893.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000675. Cutinase.
[Graphical view]
PfamiPF01083. Cutinase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiAXE2_PENPU
AccessioniPrimary (citable) accession number: O59893
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: August 1, 1998
Last modified: April 1, 2015
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.