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Protein

Endo-1,4-beta-xylanase

Gene
N/A
Organism
Penicillium simplicissimum
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.

Pathway: xylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei132 – 1321Proton donor
Active sitei238 – 2381Nucleophile

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16225.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH10. Glycoside Hydrolase Family 10.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase (EC:3.2.1.8)
Short name:
Xylanase
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase
OrganismiPenicillium simplicissimum
Taxonomic identifieri69488 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 302302Endo-1,4-beta-xylanasePRO_0000184067Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11Pyrrolidone carboxylic acid
Disulfide bondi256 ↔ 262

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
302
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 116Combined sources
Turni12 – 143Combined sources
Beta strandi16 – 227Combined sources
Helixi24 – 285Combined sources
Beta strandi29 – 313Combined sources
Helixi32 – 409Combined sources
Beta strandi42 – 487Combined sources
Helixi52 – 554Combined sources
Helixi65 – 7612Combined sources
Beta strandi80 – 878Combined sources
Beta strandi89 – 913Combined sources
Helixi94 – 974Combined sources
Helixi102 – 11918Combined sources
Turni120 – 1234Combined sources
Beta strandi125 – 1328Combined sources
Beta strandi138 – 1403Combined sources
Helixi144 – 1485Combined sources
Helixi152 – 16413Combined sources
Beta strandi168 – 1758Combined sources
Helixi183 – 19715Combined sources
Beta strandi204 – 2074Combined sources
Helixi216 – 2183Combined sources
Helixi219 – 2279Combined sources
Beta strandi232 – 24110Combined sources
Helixi246 – 25712Combined sources
Beta strandi262 – 2687Combined sources
Helixi272 – 2743Combined sources
Helixi278 – 2803Combined sources
Beta strandi283 – 2853Combined sources
Helixi293 – 3019Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B30X-ray2.25A2-302[»]
1B31X-ray1.75A1-302[»]
1B3VX-ray2.40A1-302[»]
1B3WX-ray2.60A2-302[»]
1B3XX-ray2.20A2-302[»]
1B3YX-ray2.45A2-302[»]
1B3ZX-ray2.30A2-302[»]
1BG4X-ray1.75A2-302[»]
ProteinModelPortaliP56588.
SMRiP56588. Positions 1-302.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56588.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. Glyco_hydro_10.
IPR031158. Glyco_hydro_10_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P56588-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
QASVSIDAKF KAHGKKYLGT IGDQYTLTKN TKNPAIIKAD FGQLTPENSM
60 70 80 90 100
KWDATEPNRG QFTFSGSDYL VNFAQSNGKL IRGHTLVWHS QLPGWVSSIT
110 120 130 140 150
DKNTLISVLK NHITTVMTRY KGKIYAWDVL NEIFNEDGSL RNSVFYNVIG
160 170 180 190 200
EDYVRIAFET ARSVDPNAKL YINDYNLDSA GYSKVNGMVS HVKKWLAAGI
210 220 230 240 250
PIDGIGSQTH LGAGAGSAVA GALNALASAG TKEIAITELD IAGASSTDYV
260 270 280 290 300
NVVNACLNQA KCVGITVWGV ADPDSWRSSS SPLLFDGNYN PKAAYNAIAN

AL
Length:302
Mass (Da):32,551
Last modified:December 15, 1998 - v1
Checksum:iEE7821FA58687FFC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF070417 Genomic DNA. Translation: AAC23574.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF070417 Genomic DNA. Translation: AAC23574.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B30X-ray2.25A2-302[»]
1B31X-ray1.75A1-302[»]
1B3VX-ray2.40A1-302[»]
1B3WX-ray2.60A2-302[»]
1B3XX-ray2.20A2-302[»]
1B3YX-ray2.45A2-302[»]
1B3ZX-ray2.30A2-302[»]
1BG4X-ray1.75A2-302[»]
ProteinModelPortaliP56588.
SMRiP56588. Positions 1-302.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.
BioCyciMetaCyc:MONOMER-16225.

Miscellaneous databases

EvolutionaryTraceiP56588.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. Glyco_hydro_10.
IPR031158. Glyco_hydro_10_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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).

Entry informationi

Entry nameiXYNA_PENSI
AccessioniPrimary (citable) accession number: P56588
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: June 24, 2015
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.