[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-107 AND 134-179, MASS SPECTROMETRY, FUNCTION, AND SUBCELLULAR LOCATION. STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400; PubMed=9406381 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The faeA genes from Aspergillus niger and Aspergillus tubingensis encode ferulic acid esterases involved in degradation of complex cell wall polysaccharides."; Appl. Environ. Microbiol. 63:4638-4644(1997).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/S1567-1356(01)00020-4; PubMed=12702357 [NCBI, ExPASy, EBI, Israel, Japan] Juge N., Williamson G., Puigserver A., Cummings N.J., Connerton I.F., Faulds C.B.; "High-level production of recombinant Aspergillus niger cinnamoyl esterase (FAEA) in the methylotrophic yeast Pichia pastoris."; FEMS Yeast Res. 1:127-132(2001).
[3]	FUNCTION, AND SUBCELLULAR LOCATION. STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400; Faulds C.B., Williamson G.; "Purification and characterisation of a ferulic acid esterase (FAE-III) from Aspergillus niger: specificity for the phenolic moiety and binding to microcrystalline cellulose."; Microbiology 140:779-787(1994).
[4]	FUNCTION. DOI=10.1016/0008-6215(94)00177-4; PubMed=7805053 [NCBI, ExPASy, EBI, Israel, Japan] Ralet M.C., Faulds C.B., Williamson G., Thibault J.F.; "Degradation of feruloylated oligosaccharides from sugar-beet pulp and wheat bran by ferulic acid esterases from Aspergillus niger."; Carbohydr. Res. 263:257-269(1994).
[5]	FUNCTION, AND ENZYME REGULATION. PubMed=9649839 [NCBI, ExPASy, EBI, Israel, Japan] Aliwan F.O., Williamson G.; "Identification of active site residues in a ferulic acid esterase (FAE-III) from Aspergillus niger."; Biochem. Soc. Trans. 26:S164-S164(1998).
[6]	INDUCTION. PubMed=10584009 [NCBI, ExPASy, EBI, Israel, Japan] de Vries R.P., Visser J.; "Regulation of the feruloyl esterase (faeA) gene from Aspergillus niger."; Appl. Environ. Microbiol. 65:5500-5503(1999).
[7]	FUNCTION, AND INDUCTION. STRAIN=ATCC 9089 / N402; DOI=10.1042/0264-6021:3630377; PubMed=11931668 [NCBI, ExPASy, EBI, Israel, Japan] de Vries R.P., vanKuyk P.A., Kester H.C., Visser J.; "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."; Biochem. J. 363:377-386(2002).

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.
CATALYTIC ACTIVITY: Feruloyl-polysaccharide + H₂O = ferulate + polysaccharide.
ENZYME REGULATION: Inhibited by the specific serine esterase inhibitor diisopropylfluorophosphate.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 5.0;
Temperature dependence: Optimum temperature is 55-60 degrees Celsius;
SUBCELLULAR LOCATION: Secreted.
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.
PTM: Glycosylated (Probable).
MASS SPECTROMETRY: Mass=29738; Mass_error=50; Method=MALDI; Range=22-281; Source=PubMed:9406381;.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Y09330; CAA70510.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF361950; AAK60631.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1USW; X-ray; 2.50 A; A=22-281.	[ExPASy / RCSB / EBI]
1UWC; X-ray; 1.08 A; A/B=22-281.	[ExPASy / RCSB / EBI]
1UZA; X-ray; 1.50 A; A/B=22-281.	[ExPASy / RCSB / EBI]
2BJH; X-ray; 2.54 A; A/B/C=22-281.	[ExPASy / RCSB / EBI]
2HL6; X-ray; 1.55 A; A/B=22-281.	[ExPASy / RCSB / EBI]
2IX9; X-ray; 1.70 A; A/B=22-281.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1USW; -.
1UWC; -.
1UZA; -.
2BJH; -.
2HL6; -.
2IX9; -.

ModBase

O42807.

Enzyme and pathway databases

BRENDA

3.1.1.73; 277.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from direct assay from UniProtKB).
GO:0030248;	Molecular function: cellulose binding (inferred from direct assay from UniProtKB).
GO:0030600;	Molecular function: feruloyl esterase activity (inferred from direct assay from UniProtKB).
GO:0004806;	Molecular function: triacylglycerol lipase activity (inferred from electronic annotation from InterPro).
GO:0016998;	Biological process: cell wall macromolecule catabolic process (inferred from direct assay from UniProtKB).
GO:0030245;	Biological process: cellulose catabolic process (inferred from direct assay from UniProtKB).
GO:0006629;	Biological process: lipid metabolic process (inferred from electronic annotation from InterPro).
GO:0045490;	Biological process: pectin catabolic process (inferred from direct assay from UniProtKB).
GO:0045493;	Biological process: xylan catabolic process (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR002921; Lipase_3.
Graphical view of domain structure.

Pfam

PF01764; Lipase_3; 1.
Pfam graphical view of domain structure.

PROSITE

PS00120; LIPASE_SER; 1.

Other

ProtoNet

O42807.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Glycoprotein; Hydrolase; Secreted; Serine esterase; Signal; Xylan degradation.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`
`CHAIN`	`22 281`	`260`	`Feruloyl esterase A.`	`PRO_0000021226`
`ACT_SITE`	`154 154`		`Charge relay system (By similarity).`
`CARBOHYD`	`100 100`		`N-linked (GlcNAc...).`
`CONFLICT`	`159 159`		`M -> L (in Ref. 1; AA sequence).`
`CONFLICT`	`174 174`		`V -> I (in Ref. 1; AA sequence).`
`CONFLICT`	`224 225`		`DE -> EQ (in Ref. 2; AAK60631).`
`STRAND`	`23 25`	`3`
`HELIX`	`29 44`	`16`
`TURN`	`45 51`	`7`
`STRAND`	`56 64`	`9`
`TURN`	`65 68`	`4`
`STRAND`	`69 76`	`8`
`TURN`	`77 80`	`4`
`STRAND`	`81 86`	`6`
`HELIX`	`92 98`	`7`
`STRAND`	`103 105`	`3`
`STRAND`	`116 118`	`3`
`HELIX`	`119 142`	`24`
`STRAND`	`146 153`	`8`
`HELIX`	`155 168`	`14`
`STRAND`	`172 180`	`9`
`HELIX`	`187 196`	`10`
`TURN`	`197 200`	`4`
`TURN`	`202 204`	`3`
`STRAND`	`206 212`	`7`
`HELIX`	`217 219`	`3`
`HELIX`	`223 225`	`3`
`STRAND`	`231 236`	`6`
`HELIX`	`242 244`	`3`
`STRAND`	`245 248`	`4`
`STRAND`	`250 252`	`3`
`HELIX`	`255 259`	`5`
`HELIX`	`266 269`	`4`

Sequence information

Length: 281 AA [This is the length of the unprocessed precursor]

Molecular weight: 30537 Da [This is the MW of the unprocessed precursor]

CRC64: 8B4322B72710BBF3 [This is a checksum on the sequence]

        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

O42807 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools