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Protein

Acetylxylan esterase 2

Gene

axe-2

Organism
Talaromyces purpureogenus (Soft rot fungus) (Penicillium purpureogenum)
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: xylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei117By similarity1
Active sitei202By similarity1
Active sitei214By similarity1

GO - Molecular functioni

GO - Biological processi

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

ESTHERipenpu-axylest. Acetylxylan_esterase.
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
OrganismiTalaromyces purpureogenus (Soft rot fungus) (Penicillium purpureogenum)
Taxonomic identifieri1266744 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeTalaromyces

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
PropeptideiPRO_000023462418 – 272 Publications10
ChainiPRO_000023462528 – 234Acetylxylan esterase 2Add BLAST207

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi29 ↔ 106
Disulfide bondi73 ↔ 79
Disulfide bondi128 ↔ 188
Disulfide bondi174 ↔ 206
Disulfide bondi198 ↔ 205
Glycosylationi207N-linked (GlcNAc...)Sequence analysis1

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

1234
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi31 – 37Combined sources7
Helixi47 – 49Combined sources3
Helixi50 – 59Combined sources10
Beta strandi64 – 67Combined sources4
Helixi77 – 79Combined sources3
Helixi84 – 105Combined sources22
Beta strandi110 – 116Combined sources7
Helixi118 – 128Combined sources11
Helixi133 – 135Combined sources3
Helixi146 – 151Combined sources6
Beta strandi152 – 159Combined sources8
Beta strandi170 – 173Combined sources4
Beta strandi175 – 177Combined sources3
Helixi191 – 193Combined sources3
Beta strandi194 – 197Combined sources4
Turni203 – 205Combined sources3
Helixi212 – 215Combined sources4
Helixi217 – 233Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BS9X-ray1.10A28-234[»]
1G66X-ray0.90A28-234[»]
2AXEX-ray1.80A28-234[»]
ProteinModelPortaliO59893.
SMRiO59893.
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/axe.
[Graphical view]
PfamiPF01083. Cutinase. 1 hit.
[Graphical view]
SMARTiSM01110. 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)DescriptionActionsGraphical viewLength
Sequence conflicti57L → I AA sequence (PubMed:8756392).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BS9X-ray1.10A28-234[»]
1G66X-ray0.90A28-234[»]
2AXEX-ray1.80A28-234[»]
ProteinModelPortaliO59893.
SMRiO59893.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERipenpu-axylest. Acetylxylan_esterase.
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/axe.
[Graphical view]
PfamiPF01083. Cutinase. 1 hit.
[Graphical view]
SMARTiSM01110. Cutinase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAXE2_TALPU
AccessioniPrimary (citable) accession number: O59893
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: August 1, 1998
Last modified: November 2, 2016
This is version 73 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

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 one 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.