Acetylxylan esterase precursor

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Q99034 (AXE1_HYPJE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 79. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Acetylxylan esterase
EC=3.1.1.72

Gene names

Name:

axe1

Organism

Hypocrea jecorina (Trichoderma reesei)

Taxonomic identifier

51453 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Hypocreaceae › Hypocrea

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase Serine esterase
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetylxylan esterase activity Inferred from electronic annotation. Source: EC carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW cellulose binding Inferred from electronic annotation. Source: InterPro hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

Potential

Propeptide

21 – 31

Potential

PRO_0000020771

Chain

32 – 302

271

Acetylxylan esterase

PRO_0000020772

Regions

Domain

266 – 302

CBM1

Region

244 – 266

Linker By similarity

Sites

Active site

121

By similarity

Amino acid modifications

Modified residue

Pyrrolidone carboxylic acid

Glycosylation

N-linked (GlcNAc...) Probable

Disulfide bond

274 ↔ 291

By similarity

Disulfide bond

285 ↔ 301

By similarity

Secondary structure

302

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q99034 [UniParc].

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

302

30,754

        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

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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z69256 mRNA. Translation: CAA93247.1.

PIR

S71334.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QOZ	X-ray	1.90	A/B	33-238	[»]

ProteinModelPortal

Q99034.

SMR

Q99034. Positions 32-238, 267-302.

ModBase

Search...

Protein family/group databases

CAZy

CBM1. Carbohydrate-Binding Module Family 1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

PhylomeDB

Q99034.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-16372.

Family and domain databases

InterPro

IPR000254. Cellulose-bd_dom_fun.
IPR000675. Cutinase.
[Graphical view]

Pfam

PF00734. CBM_1. 1 hit.
PF01083. Cutinase. 1 hit.
[Graphical view]

ProDom

PD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00236. fCBD. 1 hit.
[Graphical view]

SUPFAM

SSF57180. CBD_fun. 1 hit.

PROSITE

PS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00120. LIPASE_SER. 1 hit. Uncertain.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AXE1_HYPJE

Accession

Primary (citable) accession number: Q99034

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

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·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents