Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q99034 (AXE1_TRIRE)

Last modified June 16, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Acetylxylan esterase
    EC=3.1.1.72
Gene names
Name: axe1
OrganismTrichoderma reesei (Hypocrea jecorina)
Taxonomic identifier51453 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Hypocreaceae › Hypocrea

Hide | Top

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

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.

Enzyme regulation

Inhibited by phenylmethylsulfonyl flouride.

Pathway

Glycan degradation; xylan degradation.

Subunit structure

Monomer.

Subcellular location

Secreted.

Post-translational modification

Glycosylated.

Sequence similarities

Belongs to the cutinase family. Acetylxylan esterase subfamily.

Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 3111 Potential
PRO_0000020771
Chain32 – 302271Acetylxylan esterase
PRO_0000020772

Regions

Domain266 – 30237CBM1
Region244 – 26623Linker By similarity

Sites

Active site1211 By similarity

Amino acid modifications

Modified residue321Pyrrolidone carboxylic acid
Glycosylation941N-linked (GlcNAc...) Probable
Disulfide bond274 ↔ 291 By similarity
Disulfide bond285 ↔ 301 By similarity

Secondary structure

1 ................................ 302
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q99034-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: BB6EDCA2971A9F2A

FASTA30230,754
        10         20         30         40         50         60 
MPSVKETLTL LLSQAFLATG SPVDGETVVK RQCPAIHVFG ARETTVSQGY GSSATVVNLV 

        70         80         90        100        110        120 
IQAHPGTTSE AIVYPACGGQ ASCGGISYAN SVVNGTNAAA AAINNFHNSC PDTQLVLVGY 

       130        140        150        160        170        180 
SQGAQIFDNA LCGGGDPGEG ITNTAVPLTA GAVSAVKAAI FMGDPRNIHG LPYNVGTCTT 

       190        200        210        220        230        240 
QGFDARPAGF VCPSASKIKS YCDAADPYCC TGNDPNVHQG YGQEYGQQAL AFINSQLSSG 

       250        260        270        280        290        300 
GSQPPGGGPT STSRPTSTRT GSSPGPTQTH WGQCGGQGWT GPTQCESGTT CQVISQWYSQ 


CL

« Hide

Hide | Top

References

[1]"Acetyl xylan esterase from Trichoderma reesei contains an active-site serine residue and a cellulose-binding domain."
Margolles-Clark E., Tenkanen M., Soederlund H., Penttilae M.
Eur. J. Biochem. 237:553-560(1996) [PubMed: 8647098] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 158-186, CHARACTERIZATION.
Strain: QM9414 / Rut C-30.
[2]"Deacetylation of xylans by acetyl esterases of Trichoderma reesei."
Poutanen K., Sundberg M., Korte H., Puls J.
Appl. Microbiol. Biotechnol. 33:506-510(1990)
Cited for: FUNCTION.
Strain: QM9414 / Rut C-30.
[3]"Purification and properties of two acetylxylan esterases of Trichoderma reesei."
Sundberg M., Poutanen K.
Biotechnol. Appl. Biochem. 13:1-11(1991)
Cited for: CHARACTERIZATION.
Strain: QM9414 / Rut C-30.
[4]"Crystallization and preliminary X-ray diffraction studies of the catalytic core of acetyl xylan esterase from Trichoderma reesei."
Hakulinen N., Tenkanen M., Rouvinen J.
Acta Crystallogr. D 54:430-432(1998) [PubMed: 9761918] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 32-238, MASS SPECTROMETRY.
[5]"Three-dimensional structure of the catalytic core of acetylxylan esterase from Trichoderma reesei: insights into the deacetylation mechanism."
Hakulinen N., Tenkanen M., Rouvinen J.
J. Struct. Biol. 132:180-190(2000) [PubMed: 11243887] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 32-238.

Hide | Top

Cross-references

Sequence databases

Z69256 mRNA. Translation: CAA93247.1.
PIRS71334.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1QOZX-ray1.90A/B33-238[»]
ModBaseSearch...

Protein family/group databases

CAZyCBM1. Carbohydrate-Binding Module Family 1.

Enzyme and pathway databases

BRENDA3.1.1.72. 280374.

Family and domain databases

InterProIPR000254. CBD_fun.
IPR000675. Cutinase.
[Graphical view]
PfamPF00734. CBM_1. 1 hit.
PF01083. Cutinase. 1 hit.
[Graphical view]
ProDomPD001821. CBD_fungal. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00236. fCBD. 1 hit.
[Graphical view]
PROSITEPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00120. LIPASE_SER. 1 hit. Uncertain.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameAXE1_TRIRE
AccessionPrimary (citable) accession number: Q99034
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents