Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P81536

- XYNA_BYSSP

UniProt

P81536 - XYNA_BYSSP

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Endo-1,4-beta-xylanase

Gene
N/A
Organism
Byssochlamys spectabilis (Paecilomyces variotii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Temperature dependencei

Thermostable.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei86 – 861NucleophilePROSITE-ProRule annotation
Active sitei178 – 1781Proton donorPROSITE-ProRule annotation

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

UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.

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
PVX
OrganismiByssochlamys spectabilis (Paecilomyces variotii)
Taxonomic identifieri264951 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesThermoascaceaeByssochlamys

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 194194Endo-1,4-beta-xylanasePRO_0000184069Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylglycine
Disulfide bondi110 ↔ 154

Keywords - PTMi

Acetylation, Disulfide bond

Structurei

Secondary structure

1
194
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 105Combined sources
Beta strandi13 – 197Combined sources
Beta strandi25 – 295Combined sources
Beta strandi34 – 396Combined sources
Beta strandi41 – 5313Combined sources
Beta strandi59 – 8123Combined sources
Turni82 – 843Combined sources
Beta strandi85 – 9612Combined sources
Turni98 – 1014Combined sources
Beta strandi102 – 1109Combined sources
Beta strandi113 – 12715Combined sources
Beta strandi130 – 14314Combined sources
Beta strandi146 – 1516Combined sources
Helixi152 – 16110Combined sources
Beta strandi168 – 18215Combined sources
Beta strandi184 – 1929Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PVXX-ray1.59A1-194[»]
ProteinModelPortaliP81536.
SMRiP81536. Positions 1-194.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81536.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P81536-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
GTTPNSEGWH DGYYYSWWSD GGGDSTYTNN SGGTYEITWG NGGNLVGGKG
60 70 80 90 100
WNPGLNARAI HFTGVYQPNG TSYLSVYGWT RNPLVEYYIV ENFGSSNPSS
110 120 130 140 150
GSTDLGTVSC DGSTYTLGQS TRYNAPSIDG TQTFNQYWSV RQDKRSSGTV
160 170 180 190
QTGCHFDAWA SAGLNVTGDH YYQIVATEGY FSSGYARITV ADVG
Length:194
Mass (Da):20,947
Last modified:June 1, 2000 - v1
Checksum:i1D5C50AA4F6EDB90
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PVX X-ray 1.59 A 1-194 [» ]
ProteinModelPortali P81536.
SMRi P81536. Positions 1-194.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00114 .

Miscellaneous databases

EvolutionaryTracei P81536.

Family and domain databases

Gene3Di 2.60.120.180. 1 hit.
InterProi IPR013320. ConA-like_dom.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view ]
Pfami PF00457. Glyco_hydro_11. 1 hit.
[Graphical view ]
PRINTSi PR00911. GLHYDRLASE11.
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The tertiary structure at 1.59 A resolution and the proposed amino acid sequence of a family-11 xylanase from the thermophilic fungus Paecilomyces varioti bainier."
    Kumar P.R., Eswaramoorthy S., Vithayathil P.J., Viswamitra M.A.
    J. Mol. Biol. 295:581-593(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS), PROTEIN SEQUENCE OF 50-58 AND 123-128.
    Strain: Bainier.

Entry informationi

Entry nameiXYNA_BYSSP
AccessioniPrimary (citable) accession number: P81536
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2000
Last modified: November 26, 2014
This is version 65 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, Direct protein sequencing

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