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P56588

- XYNA_PENSI

UniProt

P56588 - XYNA_PENSI

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Protein

Endo-1,4-beta-xylanase

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

Functioni

Catalytic activityi

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

Pathwayi

Sites

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

GO - Molecular functioni

  1. endo-1,4-beta-xylanase activity Source: UniProtKB-EC

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB-UniPathway
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

  1. extracellular region Source: UniProtKB-SubCell
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 – 116
Turni12 – 143
Beta strandi16 – 227
Helixi24 – 285
Beta strandi29 – 313
Helixi32 – 409
Beta strandi42 – 487
Helixi52 – 554
Helixi65 – 7612
Beta strandi80 – 878
Beta strandi89 – 913
Helixi94 – 974
Helixi102 – 11918
Turni120 – 1234
Beta strandi125 – 1328
Beta strandi138 – 1403
Helixi144 – 1485
Helixi152 – 16413
Beta strandi168 – 1758
Helixi183 – 19715
Beta strandi204 – 2074
Helixi216 – 2183
Helixi219 – 2279
Beta strandi232 – 24110
Helixi246 – 25712
Beta strandi262 – 2687
Helixi272 – 2743
Helixi278 – 2803
Beta strandi283 – 2853
Helixi293 – 3019

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP56588.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. Glyco_hydro_10.
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

QASVSIDAKF KAHGKKYLGT IGDQYTLTKN TKNPAIIKAD FGQLTPENSM    50
KWDATEPNRG QFTFSGSDYL VNFAQSNGKL IRGHTLVWHS QLPGWVSSIT 100
DKNTLISVLK NHITTVMTRY KGKIYAWDVL NEIFNEDGSL RNSVFYNVIG 150
EDYVRIAFET ARSVDPNAKL YINDYNLDSA GYSKVNGMVS HVKKWLAAGI 200
PIDGIGSQTH LGAGAGSAVA GALNALASAG TKEIAITELD IAGASSTDYV 250
NVVNACLNQA KCVGITVWGV ADPDSWRSSS SPLLFDGNYN PKAAYNAIAN 300
AL 302
Length:302
Mass (Da):32,551
Last modified:December 15, 1998 - v1
Checksum:iEE7821FA58687FFC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF070417 Genomic DNA. Translation: AAC23574.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF070417 Genomic DNA. Translation: AAC23574.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B30 X-ray 2.25 A 2-302 [» ]
1B31 X-ray 1.75 A 1-302 [» ]
1B3V X-ray 2.40 A 1-302 [» ]
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 [» ]
ProteinModelPortali P56588.
SMRi P56588. Positions 1-302.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00114 .
BioCyci MetaCyc:MONOMER-16225.

Miscellaneous databases

EvolutionaryTracei P56588.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00331. Glyco_hydro_10. 1 hit.
[Graphical view ]
PRINTSi PR00134. GLHYDRLASE10.
SMARTi SM00633. Glyco_10. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 74 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

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