P56588 (XYNA_PENSI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Endo-1,4-beta-xylanase Short name=Xylanase EC=3.2.1.8 Alternative name(s): 1,4-beta-D-xylan xylanohydrolase
Organism	Penicillium simplicissimum
Taxonomic identifier	69488 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Penicillium

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Pathway	Glycan degradation; xylan degradation.
Subunit structure	Monomer.
Subcellular location	Secreted.
Sequence similarities	Belongs to the glycosyl hydrolase 10 (cellulase F) family.

Ontologies

Keywords
Biological process	Xylan degradation
Cellular component	Secreted
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Pyrrolidone carboxylic acid
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	endo-1,4-beta-xylanase 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

Chain

1 – 302

302

Endo-1,4-beta-xylanase

PRO_0000184067

Sites

Active site

132

1

Proton donor

Active site

238

1

Nucleophile

Amino acid modifications

Modified residue

1

1

Pyrrolidone carboxylic acid

Disulfide bond

256 ↔ 262

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

302

Helix Strand Turn

Details...

Helix

6 – 11

6

Turn

12 – 14

3

Beta strand

16 – 22

7

Helix

24 – 28

5

Beta strand

29 – 31

3

Helix

32 – 40

9

Beta strand

42 – 48

7

Helix

52 – 55

4

Helix

65 – 76

12

Beta strand

80 – 87

8

Beta strand

89 – 91

3

Helix

94 – 97

4

Helix

102 – 119

18

Turn

120 – 123

4

Beta strand

125 – 132

8

Beta strand

138 – 140

3

Helix

144 – 148

5

Helix

152 – 164

13

Beta strand

168 – 175

8

Helix

183 – 197

15

Beta strand

204 – 207

4

Helix

216 – 218

3

Helix

219 – 227

9

Beta strand

232 – 241

10

Helix

246 – 257

12

Beta strand

262 – 268

7

Helix

272 – 274

3

Helix

278 – 280

3

Beta strand

283 – 285

3

Helix

293 – 301

9

Sequences

	Sequence		Length	Mass (Da)
	P56588 [UniParc]. Last modified December 15, 1998. Version 1. Checksum: EE7821FA58687FFC	FASTA	302	32,551
	10 20 30 40 50 60 QASVSIDAKF KAHGKKYLGT IGDQYTLTKN TKNPAIIKAD FGQLTPENSM KWDATEPNRG 70 80 90 100 110 120 QFTFSGSDYL VNFAQSNGKL IRGHTLVWHS QLPGWVSSIT DKNTLISVLK NHITTVMTRY 130 140 150 160 170 180 KGKIYAWDVL NEIFNEDGSL RNSVFYNVIG EDYVRIAFET ARSVDPNAKL YINDYNLDSA 190 200 210 220 230 240 GYSKVNGMVS HVKKWLAAGI PIDGIGSQTH LGAGAGSAVA GALNALASAG TKEIAITELD 250 260 270 280 290 300 IAGASSTDYV NVVNACLNQA KCVGITVWGV ADPDSWRSSS SPLLFDGNYN PKAAYNAIAN AL

References

[1]	"Structure of the xylanase from Penicillium simplicissimum." Schmidt A., Schlacher A., Steiner W., Schwab H., Kratky C. Protein Sci. 7:2081-2088(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS). Strain: BT 2246.
[2]	"Xylan binding subsite mapping in the xylanase from Penicillium simplicissimum using xylooligosaccharides as cryo-protectant." Schmidt A., Gubitz G.M., Kratky C. Biochemistry 38:2403-2412(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF070417 Genomic DNA. Translation: AAC23574.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B30	X-ray	2.25	A	2-302	[»]
1B31	X-ray	1.75	A	2-302	[»]
1B3V	X-ray	2.40	A	2-302	[»]
1B3W	X-ray	2.60	A	2-302	[»]
1B3X	X-ray	2.20	A	2-302	[»]
1B3Y	X-ray	2.45	A	2-302	[»]
1B3Z	X-ray	2.30	A	2-302	[»]
1BG4	X-ray	1.75	A	2-302	[»]

ProteinModelPortal

P56588.

SMR

P56588. Positions 1-302.

ModBase

Search...

Protein family/group databases

CAZy

GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-16225.

UniPathway

UPA00114.

Family and domain databases

Gene3D

3.20.20.80. 1 hit.

InterPro

IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Pfam

PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]

PRINTS

PR00134. GLHYDRLASE10.

SMART

SM00633. Glyco_10. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P56588.

Entry information

Entry name

XYNA_PENSI

Accession

Primary (citable) accession number: P56588

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	December 15, 1998
Last modified:	May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program