Reviewed, UniProtKB/Swiss-Prot O59893 (AXE2_PENPU)

Names and origin

Protein names

Recommended name:
    Acetylxylan esterase 2
    EC=3.1.1.72
Alternative name(s):
    AXE II

Gene names

Name:	axe-2
Synonyms:	axeII

Organism

Penicillium purpurogenum

Taxonomic identifier

28575 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	234 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.
Pathway	Glycan degradation; xylan degradation.
Subunit structure	Monomer.
Subcellular location	Secreted. Ref.2
Induction	Induced by xylan and repressed by glucose. Expressed at neutral pH, but not under alkaline or acidic condtions. Ref.3
Sequence similarities	Belongs to the cutinase family. Acetylxylan esterase subfamily.
biophysicochemical properties	pH dependence: Optimum pH is 6. Temperature dependence: Optimum temperature is 60 degrees Celsius.

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
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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Potential

Propeptide

18 – 27

10

Ref.2 Ref.1

PRO_0000234624

Chain

28 – 234

207

Acetylxylan esterase 2

PRO_0000234625

Sites

Active site

117

1

By similarity

Active site

202

1

By similarity

Active site

214

1

By similarity

Amino acid modifications

Glycosylation

207

1

N-linked (GlcNAc...) Potential

Disulfide bond

29 ↔ 106

Disulfide bond

73 ↔ 79

Disulfide bond

128 ↔ 188

Disulfide bond

174 ↔ 206

Disulfide bond

198 ↔ 205

Experimental info

Sequence conflict

57

1

L → I AA sequence Ref.2

Secondary structure

1

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234

Helix Strand Turn

Details...

Beta strand

31 – 37

7

Helix

47 – 49

3

Helix

50 – 59

10

Beta strand

64 – 67

4

Helix

77 – 79

3

Helix

84 – 105

22

Beta strand

110 – 116

7

Helix

118 – 128

11

Helix

133 – 135

3

Helix

146 – 151

6

Beta strand

152 – 159

8

Beta strand

170 – 173

4

Helix

191 – 193

3

Beta strand

194 – 197

4

Turn

203 – 205

3

Helix

211 – 214

4

Helix

217 – 233

17

Sequences

	Sequence		Length	Mass (Da)
	O59893-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: C033B3DA4E7BB6E1	FASTA	234	23,478
	10 20 30 40 50 60 MHSKFFAASL LGLGAAAIPL EGVMEKRSCP AIHVFGARET TASPGYGSSS TVVNGVLSAY 70 80 90 100 110 120 PGSTAEAINY PACGGQSSCG GASYSSSVAQ GIAAVASAVN SFNSQCPSTK IVLVGYSQGG 130 140 150 160 170 180 EIMDVALCGG GDPNQGYTNT AVQLSSSAVN MVKAAIFMGD PMFRAGLSYE VGTCAAGGFD 190 200 210 220 230 QRPAGFSCPS AAKIKSYCDA SDPYCCNGSN AATHQGYGSE YGSQALAFVK SKLG

References

[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: 9506837] [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: 8756392] [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: 15174310] [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: 10089308] [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: 11134051] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (0.9 ANGSTROMS) OF 28-234.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF015285 mRNA. Translation: AAC39371.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

3.1.1.72. 15237.

Family and domain databases

InterPro

IPR000675. Cutinase.
[Graphical view]

Pfam

PF01083. Cutinase. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AXE2_PENPU

Accession

Primary (citable) accession number: O59893

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	August 1, 1998
Last modified:	June 16, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)