Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O59893

- AXE2_PENPU

UniProt

O59893 - AXE2_PENPU

Protein

Acetylxylan esterase 2

Gene

axe-2

Organism
Penicillium purpurogenum (Soft rot fungus) (Talaromyces purpurogenus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16378.
    BRENDAi3.1.1.72. 4635.
    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

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    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 – 377
    Helixi47 – 493
    Helixi50 – 5910
    Beta strandi64 – 674
    Helixi77 – 793
    Helixi84 – 10522
    Beta strandi110 – 1167
    Helixi118 – 12811
    Helixi133 – 1353
    Helixi146 – 1516
    Beta strandi152 – 1598
    Beta strandi170 – 1734
    Beta strandi175 – 1773
    Helixi191 – 1933
    Beta strandi194 – 1974
    Turni203 – 2053
    Helixi212 – 2154
    Helixi217 – 23317

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MHSKFFAASL LGLGAAAIPL EGVMEKRSCP AIHVFGARET TASPGYGSSS    50
    TVVNGVLSAY PGSTAEAINY PACGGQSSCG GASYSSSVAQ GIAAVASAVN 100
    SFNSQCPSTK IVLVGYSQGG EIMDVALCGG GDPNQGYTNT AVQLSSSAVN 150
    MVKAAIFMGD PMFRAGLSYE VGTCAAGGFD QRPAGFSCPS AAKIKSYCDA 200
    SDPYCCNGSN AATHQGYGSE YGSQALAFVK SKLG 234
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF015285 mRNA. Translation: AAC39371.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF015285 mRNA. Translation: AAC39371.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BS9 X-ray 1.10 A 28-234 [» ]
    1G66 X-ray 0.90 A 28-234 [» ]
    2AXE X-ray 1.80 A 28-234 [» ]
    ProteinModelPortali O59893.
    SMRi O59893. Positions 28-234.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    mycoCLAPi AXE5B_PENPU.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00114 .
    BioCyci MetaCyc:MONOMER-16378.
    BRENDAi 3.1.1.72. 4635.

    Miscellaneous databases

    EvolutionaryTracei O59893.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR000675. Cutinase.
    [Graphical view ]
    Pfami PF01083. Cutinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    ProtoNeti Search...

    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: October 1, 2014
    This is version 61 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