Feruloyl esterase A precursor - Aspergillus niger

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O42807 (FAEA_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 72. History...

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

Documents (2) |

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:
Feruloyl esterase A
EC=3.1.1.73

Alternative name(s):
Cinnamoyl esterase
FAE-III
Ferulic acid esterase A

Gene names

Name:

faeA

Organism

Aspergillus niger

Taxonomic identifier

5061 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	281 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	Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-galactose ester bond in pectin. Binds to cellulose. Ref.1 Ref.5 Ref.6 Ref.7 Ref.9 Ref.11 Ref.13
Catalytic activity	Feruloyl-polysaccharide + H₂O = ferulate + polysaccharide.
Enzyme regulation	Inhibited by the specific serine esterase inhibitor diisopropylfluorophosphate. Ref.7
Subcellular location	Secreted Ref.1 Ref.5.
Induction	By xylose and arabinose, probably via the xylanolytic transcriptional activator XlnR. By ferulic acid, vanillic acid and other aromatic residues with the following substituants on the aromatic ring: a methoxy group at C-3, a hydroxy group at C-4 and an unsubstituted C-5. Repressed by simple sugars, probably via the carbon catabolite repressor protein CreA. Ref.7 Ref.8 Ref.9
Post-translational modification	Glycosylated Probable. Ref.13
Sequence similarities	Belongs to the faeA family.
Biophysicochemical properties	Kinetic parameters: K_M=0.31 mM for methyl ferulate Ref.13 pH dependence: Optimum pH is 5.0. Temperature dependence: Optimum temperature is 55-60 degrees Celsius.
Mass spectrometry	Molecular mass is 29738±50 Da from positions 22 - 281. Determined by MALDI. Ref.1

Ontologies

Keywords
Biological process	Xylan degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase Serine esterase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall macromolecule catabolic process Inferred from direct assay Ref.1. Source: UniProtKB cellulose catabolic process Inferred from direct assay Ref.1. Source: UniProtKB lipid metabolic process Inferred from electronic annotation. Source: InterPro pectin catabolic process Inferred from direct assay Ref.1. Source: UniProtKB xylan catabolic process Inferred from direct assay Ref.1. Source: UniProtKB
Cellular component	extracellular region Inferred from direct assay Ref.1. Source: UniProtKB
Molecular function	carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW cellulose binding Inferred from direct assay Ref.1. Source: UniProtKB feruloyl esterase activity Inferred from direct assay Ref.1. Source: UniProtKB triglyceride lipase activity 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 – 21

Ref.1

Chain

22 – 281

260

Feruloyl esterase A

PRO_0000021226

Sites

Active site

154

Charge relay system By similarity

Active site

215

Charge relay system By similarity

Active site

268

Charge relay system By similarity

Binding site

Substrate

Binding site

101

Substrate

Binding site

268

Substrate

Amino acid modifications

Glycosylation

100

N-linked (GlcNAc...)

Disulfide bond

50 ↔ 279

Disulfide bond

112 ↔ 115

Disulfide bond

248 ↔ 255

Experimental info

Mutagenesis

101

Y → V or S: Decreases feruloyl esterase activity. Ref.12

Mutagenesis

154

S → A: Impairs catalytic activity. Ref.11

Mutagenesis

281

W → V or S: Decreases feruloyl esterase activity. Ref.12

Sequence conflict

L → S in ACJ64498. Ref.3

Sequence conflict

S → F in ACZ95366. Ref.4

Sequence conflict

A → P in ACZ95366. Ref.4

Sequence conflict

I → T in ACJ64498. Ref.3

Sequence conflict

107

D → E in ACJ64498. Ref.3

Sequence conflict

113

N → S in ACJ64498. Ref.3

Sequence conflict

128

V → I in ACJ64498. Ref.3

Sequence conflict

142

Q → K in ACZ95366. Ref.4

Sequence conflict

150

V → M in ACJ64498. Ref.3

Sequence conflict

159

M → L AA sequence Ref.1

Sequence conflict

174

V → I AA sequence Ref.1

Sequence conflict

205

T → I in ACZ95366. Ref.4

Sequence conflict

208

F → S in ACJ64498. Ref.3

Sequence conflict

224

D → E in AAK60631. Ref.2

Sequence conflict

224

D → E in ACJ64498. Ref.3

Sequence conflict

224

D → E in ACZ95366. Ref.4

Sequence conflict

225

E → Q in AAK60631. Ref.2

Sequence conflict

225

E → Q in ACJ64498. Ref.3

Sequence conflict

264

V → A in ACJ64498. Ref.3

Secondary structure

281

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

O42807 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 8B4322B72710BBF3
Show »

FASTA

281

30,537

        10         20         30         40         50         60 
MKQFSAKYAL ILLATAGQAL AASTQGISED LYNRLVEMAT ISQAAYADLC NIPSTIIKGE 

        70         80         90        100        110        120 
KIYNAQTDIN GWILRDDTSK EIITVFRGTG SDTNLQLDTN YTLTPFDTLP QCNDCEVHGG 

       130        140        150        160        170        180 
YYIGWISVQD QVESLVKQQA SQYPDYALTV TGHSLGASMA ALTAAQLSAT YDNVRLYTFG 

       190        200        210        220        230        240 
EPRSGNQAFA SYMNDAFQVS SPETTQYFRV THSNDGIPNL PPADEGYAHG GVEYWSVDPY 

       250        260        270        280 
SAQNTFVCTG DEVQCCEAQG GQGVNDAHTT YFGMTSGACT W

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References

[1]	"The faeA genes from Aspergillus niger and Aspergillus tubingensis encode ferulic acid esterases involved in degradation of complex cell wall polysaccharides." de Vries R.P., Michelsen B., Poulsen C.H., Kroon P.A., van den Heuvel R.H.H., Faulds C.B., Williamson G., van den Hombergh J.P.T.W., Visser J. Appl. Environ. Microbiol. 63:4638-4644(1997) [PubMed: 9406381] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-107 AND 134-179, MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION. Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
[2]	"High-level production of recombinant Aspergillus niger cinnamoyl esterase (FAEA) in the methylotrophic yeast Pichia pastoris." Juge N., Williamson G., Puigserver A., Cummings N.J., Connerton I.F., Faulds C.B. FEMS Yeast Res. 1:127-132(2001) [PubMed: 12702357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Cloning and directed evolution of feruloyl esterase from Aspergillus niger." Zhang S., Pei X., Wu Z. Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: CIB423.1.
[4]	"Molecular docking of feruloyl esterase A and ferulic acid substrate using computer modeling." Hu X.S., Li X.L. Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"Purification and characterisation of a ferulic acid esterase (FAE-III) from Aspergillus niger: specificity for the phenolic moiety and binding to microcrystalline cellulose." Faulds C.B., Williamson G. Microbiology 140:779-787(1994) Cited for: FUNCTION, SUBCELLULAR LOCATION. Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
[6]	"Degradation of feruloylated oligosaccharides from sugar-beet pulp and wheat bran by ferulic acid esterases from Aspergillus niger." Ralet M.C., Faulds C.B., Williamson G., Thibault J.F. Carbohydr. Res. 263:257-269(1994) [PubMed: 7805053] [Abstract] Cited for: FUNCTION.
[7]	"Identification of active site residues in a ferulic acid esterase (FAE-III) from Aspergillus niger." Aliwan F.O., Williamson G. Biochem. Soc. Trans. 26:S164-S164(1998) [PubMed: 9649839] [Abstract] Cited for: FUNCTION, ENZYME REGULATION.
[8]	"Regulation of the feruloyl esterase (faeA) gene from Aspergillus niger." de Vries R.P., Visser J. Appl. Environ. Microbiol. 65:5500-5503(1999) [PubMed: 10584009] [Abstract] Cited for: INDUCTION.
[9]	"The Aspergillus niger faeB gene encodes a second feruloyl esterase involved in pectin and xylan degradation and is specifically induced in the presence of aromatic compounds." de Vries R.P., vanKuyk P.A., Kester H.C., Visser J. Biochem. J. 363:377-386(2002) [PubMed: 11931668] [Abstract] Cited for: FUNCTION, INDUCTION. Strain: ATCC 9089 / N402.
[10]	"Structure of a feruloyl esterase from Aspergillus niger." McAuley K.E., Svendsen A., Patkar S.A., Wilson K.S. Acta Crystallogr. D 60:878-887(2004) [PubMed: 15103133] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) OF 22-281 IN COMPLEX WITH FERULIC ACID.
[11]	"The crystal structure of feruloyl esterase A from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family." Hermoso J.A., Sanz-Aparicio J., Molina R., Juge N., Gonzalez R., Faulds C.B. J. Mol. Biol. 338:495-506(2004) [PubMed: 15081808] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-281, DISULFID BONDS, FUNCTION, MUTAGENESIS OF SER-154.
[12]	"Probing the determinants of substrate specificity of a feruloyl esterase, AnFaeA, from Aspergillus niger." Faulds C.B., Molina R., Gonzalez R., Husband F., Juge N., Sanz-Aparicio J., Hermoso J.A. FEBS J. 272:4362-4371(2005) [PubMed: 16128806] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 22-281 OF MUTANT SER-154 IN COMPLEX WITH SUBSTRATE, MUTAGENESIS OF TYR-101 AND TRP-281.
[13]	"Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A." Benoit I., Asther M., Sulzenbacher G., Record E., Marmuse L., Parsiegla G., Gimbert I., Asther M., Bignon C. FEBS Lett. 580:5815-5821(2006) [PubMed: 17027758] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 22-281, GLYCOSYLATION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y09330 Genomic DNA. Translation: CAA70510.1.
AF361950 mRNA. Translation: AAK60631.1.
FJ430154 mRNA. Translation: ACJ64498.1.
GU188042 mRNA. Translation: ACZ95366.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1USW	X-ray	2.50	A	22-281	[»]
1UWC	X-ray	1.08	A/B	22-281	[»]
1UZA	X-ray	1.50	A/B	22-281	[»]
2BJH	X-ray	2.54	A/B/C	22-281	[»]
2HL6	X-ray	1.55	A/B	22-281	[»]
2IX9	X-ray	1.70	A/B	22-281	[»]

ProteinModelPortal

O42807.

SMR

O42807. Positions 22-281.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

3.1.1.73. 518.

Family and domain databases

InterPro

IPR002921. Lipase_3.
[Graphical view]

Pfam

PF01764. Lipase_3. 1 hit.
[Graphical view]

PROSITE

PS00120. LIPASE_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

FAEA_ASPNG

Accession

Primary (citable) accession number: O42807
Secondary accession number(s): B8XRG2, D2K873, Q96W70

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2001
Last sequence update:	June 1, 1998
Last modified:	June 28, 2011
This is version 72 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

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

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents