SubmitCancel

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 – 861Nucleophile By similarity
Active sitei178 – 1781Proton donor By similarity

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-xylanase
PRO_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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PVXX-ray1.59A1-194[»]
ProteinModelPortaliP81536.
SMRiP81536. Positions 1-194.

Miscellaneous databases

EvolutionaryTraceiP81536.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR008985. ConA-like_lec_gl_sf.
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

GTTPNSEGWH DGYYYSWWSD GGGDSTYTNN SGGTYEITWG NGGNLVGGKG    50
WNPGLNARAI HFTGVYQPNG TSYLSVYGWT RNPLVEYYIV ENFGSSNPSS 100
GSTDLGTVSC DGSTYTLGQS TRYNAPSIDG TQTFNQYWSV RQDKRSSGTV 150
QTGCHFDAWA SAGLNVTGDH YYQIVATEGY FSSGYARITV ADVG 194
Length:194
Mass (Da):20,947
Last modified:June 1, 2000 - v1
Checksum:i1D5C50AA4F6EDB90
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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 IPR008985. ConA-like_lec_gl_sf.
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 13, 2013
This is version 62 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

Similar proteinsi